{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,13]],"date-time":"2026-03-13T20:52:14Z","timestamp":1773435134072,"version":"3.50.1"},"reference-count":83,"publisher":"Elsevier BV","issue":"22","license":[{"start":{"date-parts":[[2020,5,1]],"date-time":"2020-05-01T00:00:00Z","timestamp":1588291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,15]],"date-time":"2020-11-15T00:00:00Z","timestamp":1605398400000},"content-version":"vor","delay-in-days":198,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM034496"],"award-info":[{"award-number":["GM034496"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2020,5]]},"DOI":"10.1074\/jbc.ra120.013336","type":"journal-article","created":{"date-parts":[[2020,4,22]],"date-time":"2020-04-22T00:45:15Z","timestamp":1587516315000},"page":"7635-7652","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"title":["The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI)"],"prefix":"10.1016","volume":"295","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6037-7710","authenticated-orcid":false,"given":"Christopher D.","family":"Radka","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4914-1440","authenticated-orcid":false,"given":"Matthew W.","family":"Frank","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7088-3468","authenticated-orcid":false,"given":"Jiangwei","family":"Yao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3942-9640","authenticated-orcid":false,"given":"Jayaraman","family":"Seetharaman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1202-511X","authenticated-orcid":false,"given":"Darcie J.","family":"Miller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8648-4189","authenticated-orcid":false,"given":"Charles O.","family":"Rock","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.013336_bib1","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/j.plipres.2013.02.002","article-title":"Bacterial lipids: Metabolism and membrane homeostasis","volume":"52","author":"Parsons","year":"2013","journal-title":"Prog. Lipid Res"},{"key":"10.1074\/jbc.RA120.013336_bib2","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1038\/35018162","article-title":"A triclosan-resistant bacterial enzyme","volume":"406","author":"Heath","year":"2000","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.013336_bib3","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1042\/bj20021699","article-title":"Characterization of Streptococcus pneumoniae enoyl-[acyl carrier protein] reductase (FabK)","volume":"370","author":"Marrakchi","year":"2003","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA120.013336_bib4","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1110\/ps.073288808","article-title":"Crystal structure of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae reveals the binding mode of an inhibitor","volume":"17","author":"Saito","year":"2008","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.RA120.013336_bib5","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1107\/S2053230X18000262","article-title":"Structural characterization of Porphyromonas gingivalis enoyl-ACP reductase II (FabK)","volume":"74","author":"Hevener","year":"2018","journal-title":"Acta Crystallogr. F Struct. Biol. Commun"},{"key":"10.1074\/jbc.RA120.013336_bib6","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0009-2797(02)00164-3","article-title":"Short-chain dehydrogenases\/reductases (SDR): The 2002 update","volume":"143\u2013144","author":"Oppermann","year":"2003","journal-title":"Chem. Biol. Interact"},{"key":"10.1074\/jbc.RA120.013336_bib7","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1146\/annurev.biochem.74.082803.133524","article-title":"The structural biology of type II fatty acid biosynthesis","volume":"74","author":"White","year":"2005","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.RA120.013336_bib8","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1042\/bj3091029","article-title":"Enoyl-acyl-carrier-protein reductase and Mycobacterium tuberculosis InhA do not conserve the Tyr-Xaa-Xaa-Xaa-Lys motif in mammalian 11\u03b2- and 17\u03b2-hydroxysteroid dehydrogenases and Drosophila alcohol dehydrogenase","volume":"309","author":"Baker","year":"1995","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA120.013336_bib9","doi-asserted-by":"crossref","first-page":"13623","DOI":"10.1021\/bi990529c","article-title":"Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis","volume":"38","author":"Parikh","year":"1999","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013336_bib10","doi-asserted-by":"crossref","first-page":"40128","DOI":"10.1074\/jbc.M005611200","article-title":"The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis","volume":"275","author":"Heath","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib11","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.jmb.2010.12.003","article-title":"Crystal structures of enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis","volume":"406","author":"Kim","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013336_bib12","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1074\/jbc.M708171200","article-title":"Vibrio cholerae fabV defines a new class of enoyl acyl-carrier-protein reductase","volume":"283","author":"Massengo-Tiass\u00e9","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib13","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1128\/AAC.01152-09","article-title":"Triclosan resistance of Pseudomonas aeruginosa PAO1 is due to FabV, a triclosan-resistant enoyl-acyl carrier protein reductase","volume":"54","author":"Zhu","year":"2010","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib14","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.str.2011.07.019","article-title":"Structure of the Yersinia pestis FabV enoyl-ACP reductase and its interaction with two 2-pyridone inhibitors","volume":"20","author":"Hirschbeck","year":"2012","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.013336_bib15","doi-asserted-by":"crossref","first-page":"26538","DOI":"10.1074\/jbc.270.44.26538","article-title":"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli","volume":"270","author":"Heath","year":"1995","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib16","doi-asserted-by":"crossref","first-page":"a027045","DOI":"10.1101\/cshperspect.a027045","article-title":"Resistance mechanisms and the future of bacterial enoyl-acyl carrier protein reductase (FabI) antibiotics","volume":"6","author":"Yao","year":"2016","journal-title":"Cold Spring Harbor Perspect. Med"},{"key":"10.1074\/jbc.RA120.013336_bib17","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1016\/j.bbalip.2016.09.014","article-title":"Bacterial fatty acid metabolism in modern antibiotic discovery","volume":"1862","author":"Yao","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Biol. Lipids"},{"key":"10.1074\/jbc.RA120.013336_bib18","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1179\/1973947812Y.0000000063","article-title":"In vitro activity (MICs and rate of kill) of AFN-1252, a novel FabI inhibitor, in the presence of serum and in combination with other antibiotics","volume":"25","author":"Kaplan","year":"2013","journal-title":"J. Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib19","doi-asserted-by":"crossref","first-page":"5865","DOI":"10.1128\/AAC.01411-12","article-title":"Mode of action, in vitro activity, and in vivo efficacy of AFN-1252, a selective antistaphylococcal FabI inhibitor","volume":"56","author":"Kaplan","year":"2012","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib20","doi-asserted-by":"crossref","first-page":"1695","DOI":"10.1128\/AAC.01741-15","article-title":"Efficacy and safety of AFN-1252, the first Staphylococcus-specific antibacterial agent, in the treatment of acute bacterial skin and skin structure infections, including those in patients with significant comorbidities","volume":"60","author":"Hafkin","year":"2015","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib21","doi-asserted-by":"crossref","first-page":"e01669","DOI":"10.1128\/AAC.01669-18","article-title":"Bone and joint tissue penetration of the Staphylococcus-selective antibiotic afabicin in patients undergoing elective hip replacement surgery","volume":"63","author":"Menetrey","year":"2019","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib22","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1146\/annurev-micro-091313-103456","article-title":"Effects of antibiotics on human microbiota and subsequent disease","volume":"68","author":"Keeney","year":"2014","journal-title":"Annu. Rev. Microbiol"},{"key":"10.1074\/jbc.RA120.013336_bib23","doi-asserted-by":"crossref","first-page":"2741","DOI":"10.1128\/IAI.00006-09","article-title":"Prolonged impact of antibiotics on intestinal microbial ecology and susceptibility to enteric Salmonella infection","volume":"77","author":"Croswell","year":"2009","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.RA120.013336_bib24","doi-asserted-by":"crossref","first-page":"4264","DOI":"10.1128\/AAC.00535-16","article-title":"A pathogen-selective antibiotic minimizes disturbance to the microbiome","volume":"60","author":"Yao","year":"2016","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib25","doi-asserted-by":"crossref","first-page":"E14","DOI":"10.3390\/microorganisms7010014","article-title":"What is the healthy gut microbiota composition? A changing ecosystem across age, environment, diet, and diseases","volume":"7","author":"Rinninella","year":"2019","journal-title":"Microorganisms"},{"key":"10.1074\/jbc.RA120.013336_bib26","doi-asserted-by":"crossref","first-page":"12514","DOI":"10.1021\/bi9907779","article-title":"Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan","volume":"38","author":"Ward","year":"1999","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013336_bib27","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1016\/j.str.2012.03.013","article-title":"Staphylococcus aureus FabI: Inhibition, substrate recognition, and potential implications for in vivo essentiality","volume":"20","author":"Schiebel","year":"2012","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.013336_bib28","doi-asserted-by":"crossref","first-page":"15582","DOI":"10.1074\/jbc.274.22.15582","article-title":"Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate","volume":"274","author":"Rozwarski","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib29","doi-asserted-by":"crossref","first-page":"22365","DOI":"10.1074\/jbc.M114.584185","article-title":"Type II fatty acid synthesis is essential for the replication of Chlamydia trachomatis","volume":"289","author":"Yao","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib30","doi-asserted-by":"crossref","first-page":"7516","DOI":"10.1021\/jm400637m","article-title":"Design, synthesis, and biological and crystallographic evaluation of novel inhibitors of Plasmodium falciparum enoyl-ACP-reductase (PfFabI)","volume":"56","author":"Belluti","year":"2013","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00109-016-1492-2","article-title":"Microbiome and metabolic disease: Revisiting the bacterial phylum Bacteroidetes","volume":"95","author":"Johnson","year":"2017","journal-title":"J. Mol. Med. (Berl.)"},{"key":"10.1074\/jbc.RA120.013336_bib32","doi-asserted-by":"crossref","first-page":"3544","DOI":"10.1128\/AAC.00400-09","article-title":"AFN-1252, a FabI inhibitor, demonstrates a Staphylococcus-specific spectrum of activity","volume":"53","author":"Karlowsky","year":"2009","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib33","doi-asserted-by":"crossref","first-page":"36261","DOI":"10.1074\/jbc.M113.512905","article-title":"Resistance to AFN-1252 arises from missense mutations in Staphylococcus aureus enoyl-acyl carrier protein reductase (FabI)","volume":"288","author":"Yao","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib34","doi-asserted-by":"crossref","first-page":"4654","DOI":"10.1074\/jbc.275.7.4654","article-title":"Inhibition of the Staphylococcus aureus NADPH-dependent enoyl-acyl carrier protein reductase by triclosan and hexachlorophene","volume":"275","author":"Heath","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib35","doi-asserted-by":"crossref","first-page":"11110","DOI":"10.1074\/jbc.274.16.11110","article-title":"Mechanism of triclosan inhibition of bacterial fatty acid synthesis","volume":"274","author":"Heath","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib36","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1107\/S2053230X15022098","article-title":"Crystallographic insights into the structure-activity relationships of diazaborine enoyl-ACP reductase inhibitors","volume":"71","author":"Jordan","year":"2015","journal-title":"Acta Crystallogr. F Struct. Biol. Cryst. Commun"},{"key":"10.1074\/jbc.RA120.013336_bib37","doi-asserted-by":"crossref","first-page":"44809","DOI":"10.1074\/jbc.M208920200","article-title":"A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae","volume":"277","author":"Marrakchi","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib38","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.bbrc.2017.09.084","article-title":"Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis","volume":"493","author":"Kim","year":"2017","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.RA120.013336_bib39","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.bbrc.2010.08.083","article-title":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus","volume":"400","author":"Kim","year":"2010","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.RA120.013336_bib40","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1002\/prot.22581","article-title":"Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP and triclosan","volume":"78","author":"Priyadarshi","year":"2010","journal-title":"Proteins"},{"key":"10.1074\/jbc.RA120.013336_bib41","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/S0969-2126(01)00227-1","article-title":"Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase","volume":"3","author":"Rafferty","year":"1995","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.013336_bib42","doi-asserted-by":"crossref","first-page":"13106","DOI":"10.1074\/jbc.M112000200","article-title":"Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase","volume":"277","author":"Perozzo","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib43","doi-asserted-by":"crossref","first-page":"14330","DOI":"10.1074\/jbc.M109.090373","article-title":"A slow, tight binding inhibitor of InhA, the enoyl-acyl carrier protein reductase from Mycobacterium tuberculosis","volume":"285","author":"Luckner","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib44","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/j.jmb.2004.08.033","article-title":"Structural basis for the variation in triclosan affinity to enoyl reductases","volume":"343","author":"Pidugu","year":"2004","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013336_bib45","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/S0969-2126(00)00064-2","article-title":"The refined three-dimensional structure of 3\u03b1,20\u03b2-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases","volume":"2","author":"Ghosh","year":"1994","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.013336_bib46","doi-asserted-by":"crossref","first-page":"7715","DOI":"10.1021\/bi951904d","article-title":"Crystal structures of the binary and ternary complexes of 7\u03b1-hydroxysteroid dehydrogenase from Escherichia coli","volume":"35","author":"Tanaka","year":"1996","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013336_bib47","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/273443a0","article-title":"The \u03b1-helix dipole and the properties of proteins","volume":"273","author":"Hol","year":"1978","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.013336_bib48","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1107\/S0907444906053625","article-title":"Studies of Toxoplasma gondiiPlasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents","volume":"63","author":"Muench","year":"2007","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013336_bib49","doi-asserted-by":"crossref","first-page":"2529","DOI":"10.1110\/ps.8.11.2529","article-title":"Molecular basis for triclosan activity involves a flipping loop in the active site","volume":"8","author":"Qiu","year":"1999","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.RA120.013336_bib50","doi-asserted-by":"crossref","first-page":"1638","DOI":"10.1126\/science.7886450","article-title":"Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis","volume":"267","author":"Dessen","year":"1995","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.013336_bib51","doi-asserted-by":"crossref","first-page":"5933","DOI":"10.1021\/jm300489v","article-title":"Structural and enzymatic analyses reveal the binding mode of a novel series of Francisella tularensis enoyl reductase (FabI) inhibitors","volume":"55","author":"Mehboob","year":"2012","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib52","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.1021\/bi5014358","article-title":"An ordered water channel in Staphylococcus aureus FabI: Unraveling the mechanism of substrate recognition and reduction","volume":"54","author":"Schiebel","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013336_bib53","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1006\/jmbi.1994.1022","article-title":"Planar stacking interactions of arginine and aromatic side-chains in proteins","volume":"235","author":"Flocco","year":"1994","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013336_bib54","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1126\/science.279.5347.98","article-title":"Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis","volume":"279","author":"Rozwarski","year":"1998","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.013336_bib55","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1186\/s13073-016-0294-z","article-title":"The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation","volume":"8","author":"Langdon","year":"2016","journal-title":"Genome Med"},{"key":"10.1074\/jbc.RA120.013336_bib56","first-page":"1543","article-title":"Antibiotics and the human gut microbiome: Dysbioses and accumulation of resistances","volume":"6","author":"Francino","year":"2015","journal-title":"Front. Microbiol"},{"key":"10.1074\/jbc.RA120.013336_bib57","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1093\/bioinformatics\/btq706","article-title":"Phangorn: Phylogenetic analysis in R","volume":"27","author":"Schliep","year":"2011","journal-title":"Bioinformatics"},{"key":"10.1074\/jbc.RA120.013336_bib58","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1186\/s12859-015-0749-z","article-title":"DECIPHER: Harnessing local sequence context to improve protein multiple sequence alignment","volume":"16","author":"Wright","year":"2015","journal-title":"BMC Bioinformatics"},{"key":"10.1074\/jbc.RA120.013336_bib59","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1093\/molbev\/msn067","article-title":"An improved general amino acid replacement matrix","volume":"25","author":"Le","year":"2008","journal-title":"Mol. Biol. Evol"},{"key":"10.1074\/jbc.RA120.013336_bib60","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1111\/2041-210X.12628","article-title":"GGTREE: An R package for visualization and annotation of phylogenetic trees with their covariates and other associated data","volume":"8","author":"Yu","year":"2017","journal-title":"Methods Ecol. Evol"},{"key":"10.1074\/jbc.RA120.013336_bib61","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1111\/mmi.14445","article-title":"Fatty acid activation and utilization by Alistipes finegoldii, a representative Bacteroidetes resident of the human gut microbiome","volume":"113","author":"Radka","year":"2020","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA120.013336_bib62","doi-asserted-by":"crossref","first-page":"15378","DOI":"10.1073\/pnas.1109208108","article-title":"Metabolic basis for the differential susceptibility of Gram-positive pathogens to fatty acid synthesis inhibitors","volume":"108","author":"Parsons","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.013336_bib63","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1128\/AAC.46.5.1246-1252.2002","article-title":"A missense mutation in the fabB (\u03b2-ketoacyl-acyl carrier protein synthase I) gene confers thiolactomycin resistance to Escherichia coli","volume":"46","author":"Jackowski","year":"2002","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA120.013336_bib64","doi-asserted-by":"crossref","first-page":"20.12.1","DOI":"10.1002\/0471140864.ps2012s71","article-title":"Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation","volume":"71","author":"Zhao","year":"2013","journal-title":"Curr. Protoc. Protein Sci"},{"key":"10.1074\/jbc.RA120.013336_bib65","series-title":"Basic Principles of Analytical Ultracentrifugation","author":"Schuck","year":"2015"},{"key":"10.1074\/jbc.RA120.013336_bib66","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1016\/S0006-3495(00)76713-0","article-title":"Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling","volume":"78","author":"Schuck","year":"2000","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.RA120.013336_bib67","doi-asserted-by":"crossref","first-page":"e0126420","DOI":"10.1371\/journal.pone.0126420","article-title":"A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation","volume":"10","author":"Zhao","year":"2015","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA120.013336_bib68","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1074\/jbc.M115.699462","article-title":"Activation of exogenous fatty acids to acyl-acyl carrier protein cannot bypass FabI inhibition in Neisseria","volume":"291","author":"Yao","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013336_bib69","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"[20] Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA120.013336_bib70","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1107\/S0907444906045975","article-title":"Solving structures of protein complexes by molecular replacement with Phaser","volume":"63","author":"McCoy","year":"2007","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013336_bib71","article-title":"Crystal structure of enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5","author":"Chen","year":"2007","journal-title":"Protein Data Bank"},{"key":"10.1074\/jbc.RA120.013336_bib72","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013336_bib73","doi-asserted-by":"crossref","first-page":"2196","DOI":"10.1107\/S0907444904019079","article-title":"Direct incorporation of experimental phase information in model refinement","volume":"60","author":"Skub\u00e1k","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013336_bib74","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: Model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013336_bib75","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2002"},{"key":"10.1074\/jbc.RA120.013336_bib76","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1107\/S2059798317015236","article-title":"The crystal structure of the Yersinia pestis iron chaperone YiuA reveals a basic triad binding motif for the chelated metal","volume":"73","author":"Radka","year":"2017","journal-title":"Acta Crystallogr. D Struct. Biol"},{"key":"10.1074\/jbc.RA120.013336_bib77","article-title":"Crystal structure of E. coli enoyl reductase in complex with NAD and AFN-1252","author":"Subramanya","year":"2013","journal-title":"Protein Data Bank"},{"key":"10.1074\/jbc.RA120.013336_bib78","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1002\/emmm.201201689","article-title":"Towards a new tuberculosis drug: Pyridomycin\u2014nature's isoniazid","volume":"4","author":"Hartkoorn","year":"2012","journal-title":"EMBO Mol. Med"},{"key":"10.1074\/jbc.RA120.013336_bib79","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1099\/00221287-138-10-2093","article-title":"Sequences of the envM gene and of two mutated alleles in Escherichia coli","volume":"138","author":"Bergler","year":"1992","journal-title":"J. Gen. Microbiol"},{"key":"10.1074\/jbc.RA120.013336_bib80","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/j.molcel.2006.06.030","article-title":"Acyl-phosphates initiate membrane phospholipid synthesis in gram-positive pathogens","volume":"23","author":"Lu","year":"2006","journal-title":"Molec. Cell"},{"key":"10.1074\/jbc.RA120.013336_bib81","doi-asserted-by":"crossref","DOI":"10.2210\/pdb5cfz\/pdb","article-title":"Crystal structure of E. coli FabI in apo form","author":"Jordan","year":"2015","journal-title":"Protein Data Bank"},{"key":"10.1074\/jbc.RA120.013336_bib82","article-title":"Mycobacterium tuberculosis InhA in complex with NADH","author":"Pojer","year":"2012","journal-title":"Protein Data Bank"},{"key":"10.1074\/jbc.RA120.013336_bib83","doi-asserted-by":"crossref","DOI":"10.2210\/pdb4q9n\/pdb","article-title":"Crystal structure of Chlamydia trachomatis enoyl-ACP reductase (FabI) in complex with NADH and AFN-1252","author":"Yao","year":"2014","journal-title":"Protein Data Bank"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817494567?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817494567?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.013336","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,18]],"date-time":"2021-12-18T05:54:30Z","timestamp":1639806870000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925817494567"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,5]]},"references-count":83,"journal-issue":{"issue":"22","published-print":{"date-parts":[[2020,5]]}},"alternative-id":["S0021925817494567"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.013336","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2020,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI)","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.013336","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Radka et al.","name":"copyright","label":"Copyright"}]}}