{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T06:36:14Z","timestamp":1790750174986,"version":"4.1.0"},"reference-count":57,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2016,6,1]],"date-time":"2016-06-01T00:00:00Z","timestamp":1464739200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,6,7]],"date-time":"2017-06-07T00:00:00Z","timestamp":1496793600000},"content-version":"vor","delay-in-days":371,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"CIHR","doi-asserted-by":"publisher","award":["MOP-13107"],"award-info":[{"award-number":["MOP-13107"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"name":"STIHR training program"},{"name":"NSERC CGS-M program"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Structure"],"published-print":{"date-parts":[[2016,6]]},"DOI":"10.1016\/j.str.2016.04.002","type":"journal-article","created":{"date-parts":[[2016,5,6]],"date-time":"2016-05-06T00:22:05Z","timestamp":1462494125000},"page":"935-945","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":12,"title":["Antibiotic Binding Drives Catalytic Activation of Aminoglycoside Kinase APH(2\u2033)-Ia"],"prefix":"10.1016","volume":"24","author":[{"given":"Shane\u00a0J.","family":"Caldwell","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yue","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Albert\u00a0M.","family":"Berghuis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.str.2016.04.002_bib1","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.micres.2005.05.002","article-title":"Investigation of aminoglycoside modifying enzyme genes in methicillin-resistant staphylococci","volume":"161","author":"Ardic","year":"2006","journal-title":"Microbiol. Res."},{"key":"10.1016\/j.str.2016.04.002_bib2","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1016\/j.str.2011.02.016","article-title":"Briefly bound to activate: transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis","volume":"1993","author":"Bao","year":"2011","journal-title":"Structure"},{"key":"10.1016\/j.str.2016.04.002_bib3","doi-asserted-by":"crossref","first-page":"4788","DOI":"10.1021\/ja312237q","article-title":"Phosphoryl transfer by protein kinase A is captured in a crystal lattice","volume":"135","author":"Bastidas","year":"2013","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.str.2016.04.002_bib4","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1107\/S0907444910048675","article-title":"iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM","volume":"67","author":"Battye","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.str.2016.04.002_bib5","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1007\/BF00293929","article-title":"Plasmid pGB301, a new\u00a0multiple resistance streptococcal cloning vehicle and its use in cloning of a gentamicin\/kanamycin resistance determinant","volume":"182","author":"Behnke","year":"1981","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.str.2016.04.002_bib6","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/S1047-8477(03)00039-X","article-title":"Seeds to crystals","volume":"142","author":"Bergfors","year":"2003","journal-title":"J.\u00a0Struct. Biol."},{"key":"10.1016\/j.str.2016.04.002_bib7","doi-asserted-by":"crossref","first-page":"9846","DOI":"10.1021\/bi049135y","article-title":"Domain-domain interactions in the aminoglycoside antibiotic resistance enzyme AAC(6\u2032)-APH(2\u2032)","volume":"43","author":"Boehr","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2016.04.002_bib8","doi-asserted-by":"crossref","first-page":"8756","DOI":"10.1021\/bi010504p","article-title":"Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase","volume":"40","author":"Burk","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2016.04.002_bib9","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.1128\/AAC.06378-11","article-title":"Small-angle X-ray scattering analysis of the bifunctional antibiotic resistance enzyme aminoglycoside\u00a0(6\u2032) acetyltransferase-Ie\/aminoglycoside (2\u2032) phosphotransferase-Ia reveals a rigid solution structure","volume":"56","author":"Caldwell","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.str.2016.04.002_bib10","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/S1074-5521(99)80006-4","article-title":"Prodigious substrate specificity of AAC(6\u2032)-APH(2\u2032), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci","volume":"6","author":"Daigle","year":"1999","journal-title":"Chem. Biol."},{"key":"10.1016\/j.str.2016.04.002_bib11","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/S0966-842X(97)01033-0","article-title":"Bacterial resistance to aminoglycoside antibiotics","volume":"5","author":"Davies","year":"1997","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.str.2016.04.002_bib12","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1128\/AAC.11.1.47","article-title":"Mechanisms of gentamicin resistance in Staphylococcus aureus","volume":"11","author":"Dowding","year":"1977","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.str.2016.04.002_bib13","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":"10.1016\/j.str.2016.04.002_bib14","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1146\/annurev-biochem-052410-090317","article-title":"The structural basis for control of eukaryotic protein kinases","volume":"81","author":"Endicott","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.str.2016.04.002_bib15","doi-asserted-by":"crossref","first-page":"2323","DOI":"10.1093\/emboj\/21.10.2323","article-title":"Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry","volume":"21","author":"Fong","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.str.2016.04.002_bib16","doi-asserted-by":"crossref","first-page":"43262","DOI":"10.1074\/jbc.M112.416453","article-title":"Revisiting the nucleotide and aminoglycoside substrate specificity of the bifunctional aminoglycoside acetyltransferase(6\u2032)-Ie\/aminoglycoside phosphotransferase(2\u2032)-Ia enzyme","volume":"287","author":"Frase","year":"2012","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2016.04.002_bib17","doi-asserted-by":"crossref","first-page":"3721","DOI":"10.1021\/bi400066a","article-title":"Insights into the phosphoryl transfer catalyzed by cAMP-dependent protein kinase: an X-ray crystallographic study of complexes with various metals and peptide substrate SP20","volume":"52","author":"Gerlits","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2016.04.002_bib18","first-page":"1811","article-title":"Aminoglycosides: a practical review","volume":"58","author":"Gonzalez","year":"1998","journal-title":"Am. Fam. Physician"},{"key":"10.1016\/j.str.2016.04.002_bib19","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/S0092-8674(00)80274-3","article-title":"Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases","volume":"89","author":"Hon","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.str.2016.04.002_bib20","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1002\/cbic.200900779","article-title":"The future of aminoglycosides: the end or renaissance?","volume":"11","author":"Houghton","year":"2010","journal-title":"Chembiochem"},{"key":"10.1016\/j.str.2016.04.002_bib21","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1126\/science.1218231","article-title":"Linking crystallographic model and data quality","volume":"336","author":"Karplus","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.str.2016.04.002_bib22","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1128\/AAC.12.1.26","article-title":"2\u2033-O-phosphorylation of gentamicin components by a Staphylococcus aureus strain carrying a plasmid","volume":"12","author":"Le Goffic","year":"1977","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.str.2016.04.002_bib23","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/j.str.2015.04.001","article-title":"Molecular basis of the activity and the regulation of the eukaryotic-like S\/T protein kinase PknG from Mycobacterium tuberculosis","volume":"1993","author":"Lisa","year":"2015","journal-title":"Structure"},{"key":"10.1016\/j.str.2016.04.002_bib24","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/nsb780","article-title":"Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase","volume":"9","author":"Madhusudan","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.str.2016.04.002_bib25","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1128\/AAC.47.5.1577-1583.2003","article-title":"Aminoglycoside resistance resulting from tight drug binding to an altered aminoglycoside acetyltransferase","volume":"47","author":"Magnet","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.str.2016.04.002_bib26","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.str.2016.04.002_bib27","doi-asserted-by":"crossref","first-page":"e00915","DOI":"10.1128\/mBio.00915-14","article-title":"Amplification of aminoglycoside resistance gene aphA1 in Acinetobacter baumannii results in tobramycin therapy failure","volume":"5","author":"McGann","year":"2014","journal-title":"MBio"},{"key":"10.1016\/j.str.2016.04.002_bib28","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/j.bbamcr.2010.11.011","article-title":"Site-directed mutagenesis of the glycine-rich loop of death associated protein kinase (DAPK) identifies it as a key structure for catalytic activity","volume":"1813","author":"McNamara","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.str.2016.04.002_bib29","doi-asserted-by":"crossref","first-page":"e1001680","DOI":"10.1371\/journal.pbio.1001680","article-title":"Deciphering the structural basis of eukaryotic protein kinase regulation","volume":"11","author":"Meharena","year":"2013","journal-title":"PLoS Biol."},{"key":"10.1016\/j.str.2016.04.002_bib30","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.str.2016.04.002_bib31","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/1472-6750-10-21","article-title":"A mutant Pfu DNA polymerase designed for advanced uracil-excision DNA engineering","volume":"10","author":"N\u00f8rholm","year":"2010","journal-title":"BMC Biotechnol."},{"key":"10.1016\/j.str.2016.04.002_bib32","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1107\/S0021889805038987","article-title":"TLSMD web server for the generation of multi-group TLS models","volume":"39","author":"Painter","year":"2006","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.str.2016.04.002_bib33","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/S0969-2126(03)00094-7","article-title":"The crystal structure of choline kinase reveals a eukaryotic protein kinase fold","volume":"1993","author":"Peisach","year":"2003","journal-title":"Structure"},{"key":"10.1016\/j.str.2016.04.002_bib34","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.abb.2007.04.004","article-title":"An intrinsic ATPase activity of phospho-MEK-1 uncoupled from downstream ERK phosphorylation","volume":"464","author":"Rominger","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.str.2016.04.002_bib35","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1111\/j.1574-695X.2012.00997.x","article-title":"Increased high-level gentamicin resistance in invasive Enterococcus faecium is associated with AAC(6\u2032)Ie-APH(2\u2032)Ia-encoding transferable megaplasmids hosted by major hospital-adapted lineages","volume":"66","author":"Rosvoll","year":"2012","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"10.1016\/j.str.2016.04.002_bib36","doi-asserted-by":"crossref","first-page":"66","DOI":"10.3181\/00379727-55-14461","article-title":"Streptomycin, a substance exhibiting antibiotic activity against gram-positive and gram-negative bacteria","volume":"55","author":"Schatz","year":"1944","journal-title":"Proc. Soc. Exp. Biol. Med."},{"key":"10.1016\/j.str.2016.04.002_bib37","doi-asserted-by":"crossref","first-page":"e49","DOI":"10.1371\/journal.pcbi.0010049","article-title":"Structural evolution of the protein kinase-like superfamily","volume":"1","author":"Scheeff","year":"2005","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.str.2016.04.002_bib38","doi-asserted-by":"crossref","first-page":"6237","DOI":"10.1021\/bi200747f","article-title":"Crystal structures of antibiotic-bound complexes of aminoglycoside 2\u2033-phosphotransferase IVa highlight the diversity in substrate binding modes among aminoglycoside kinases","volume":"50","author":"Shi","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2016.04.002_bib39","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1107\/S1399004714005331","article-title":"Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6\u2032)-Ie-APH(2\u2032)-Ia","volume":"70","author":"Smith","year":"2014","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.str.2016.04.002_bib40","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.1107\/S1399004714017635","article-title":"Structure of the bifunctional aminoglycoside-resistance enzyme AAC(6\u2032)-Ie-APH(2\u2032)-Ia revealed by crystallographic and small-angle X-ray scattering analysis","volume":"70","author":"Smith","year":"2014","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.str.2016.04.002_bib41","doi-asserted-by":"crossref","first-page":"e01998","DOI":"10.7554\/eLife.01998","article-title":"Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6","volume":"3","author":"Stamos","year":"2014","journal-title":"Elife"},{"key":"10.1016\/j.str.2016.04.002_bib42","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.pep.2005.01.016","article-title":"Protein production by auto-induction in high density shaking cultures","volume":"41","author":"Studier","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.str.2016.04.002_bib43","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.bbapap.2003.11.029","article-title":"PKA: a portrait of protein kinase dynamics","volume":"1697","author":"Taylor","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.str.2016.04.002_bib44","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1038\/nsb1001-899","article-title":"Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression","volume":"8","author":"Tereshko","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.str.2016.04.002_bib45","doi-asserted-by":"crossref","first-page":"2016","DOI":"10.1002\/pro.209","article-title":"Comparative surface geometry of the protein kinase family","volume":"18","author":"Thompson","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.str.2016.04.002_bib46","doi-asserted-by":"crossref","first-page":"6690","DOI":"10.1074\/jbc.M808148200","article-title":"Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2\u2033-phosphotransferases","volume":"284","author":"Toth","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2016.04.002_bib47","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1128\/AAC.02049-12","article-title":"Novel aminoglycoside 2\u2033-phosphotransferase identified in a gram-negative pathogen","volume":"57","author":"Toth","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.str.2016.04.002_bib48","doi-asserted-by":"crossref","first-page":"12074","DOI":"10.1021\/ja1046439","article-title":"Role of aromatic rings in the molecular recognition of aminoglycoside antibiotics: implications for drug design","volume":"132","author":"Vacas","year":"2010","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.str.2016.04.002_bib49","doi-asserted-by":"crossref","first-page":"9825","DOI":"10.1021\/bi800664x","article-title":"Mechanistic and structural analysis of aminoglycoside N-acetyltransferase AAC(6\u2032)-Ib and its bifunctional, fluoroquinolone-active AAC(6\u2032)-Ib-cr variant","volume":"47","author":"Vetting","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2016.04.002_bib50","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1002\/bip.10414","article-title":"Molecular recognition of aminoglycoside antibiotics by ribosomal RNA and resistance enzymes: an analysis of x-ray crystal structures","volume":"70","author":"Vicens","year":"2003","journal-title":"Biopolymers"},{"key":"10.1016\/j.str.2016.04.002_bib51","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/B978-0-12-397918-6.00001-X","article-title":"Catalytic mechanisms and regulation of protein kinases","volume":"548","author":"Wang","year":"2014","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.str.2016.04.002_bib52","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP 4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.str.2016.04.002_bib53","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/nsmb.1388","article-title":"Structural and biochemical characterization of the KRLB region in insulin receptor substrate-2","volume":"15","author":"Wu","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.str.2016.04.002_bib54","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1089\/mdr.2009.0897","article-title":"Prevalence of the genes encoding aminoglycoside-modifying enzymes and methicillin resistance among clinical isolates of Staphylococcus aureus in Tehran, Iran","volume":"15","author":"Yadegar","year":"2009","journal-title":"Microb. Drug Resist."},{"key":"10.1016\/j.str.2016.04.002_bib55","doi-asserted-by":"crossref","first-page":"4133","DOI":"10.1128\/JB.00149-09","article-title":"The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside-2\u2032-phosphotransferase-IIa [APH(2\u2032)-IIa] provide insights into substrate selectivity in the APH(2\u2032) subfamily","volume":"191","author":"Young","year":"2009","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.str.2016.04.002_bib56","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.sbi.2014.05.008","article-title":"Resilience of biochemical activity in protein domains in the face of structural divergence","volume":"26C","author":"Zhang","year":"2014","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.str.2016.04.002_bib57","doi-asserted-by":"crossref","first-page":"2154","DOI":"10.1021\/bi00060a005","article-title":"Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor","volume":"32","author":"Zheng","year":"1993","journal-title":"Biochemistry"}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212616300387?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212616300387?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,12]],"date-time":"2018-09-12T11:57:04Z","timestamp":1536753424000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212616300387"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,6]]},"references-count":57,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2016,6]]}},"alternative-id":["S0969212616300387"],"URL":"https:\/\/doi.org\/10.1016\/j.str.2016.04.002","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[2016,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Antibiotic Binding Drives Catalytic Activation of Aminoglycoside Kinase APH(2\u2033)-Ia","name":"articletitle","label":"Article Title"},{"value":"Structure","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.str.2016.04.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}