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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2019,10,29]]},"abstract":"<jats:p>\n                    Resistance to antibiotics has become a major threat to modern medicine. The ribosome plays a fundamental role in cell vitality by the translation of the genetic code into proteins; hence, it is a major target for clinically useful antibiotics. We report here the cryo-electron microscopy structures of the ribosome of a pathogenic aminoglycoside (AG)-resistant\n                    <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                    strain, as well as of a nonresistance strain isolated from a cystic fibrosis patient. The structural studies disclosed defective ribosome complex formation due to a conformational change of rRNA helix H69, an essential intersubunit bridge, and a secondary binding site of the AGs. In addition, a stable conformation of nucleotides A1486 and A1487, pointing into helix h44, is created compared to a non-AG-bound ribosome. We suggest that altering the conformations of ribosomal protein uL6 and rRNA helix H69, which interact with initiation-factor IF2, interferes with proper protein synthesis initiation.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1909831116","type":"journal-article","created":{"date-parts":[[2019,10,14]],"date-time":"2019-10-14T20:54:16Z","timestamp":1571086456000},"page":"22275-22281","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":40,"title":["Structure of\n                    <i>Pseudomonas aeruginosa<\/i>\n                    ribosomes from an aminoglycoside-resistant clinical isolate"],"prefix":"10.1073","volume":"116","author":[{"given":"Yehuda","family":"Halfon","sequence":"first","affiliation":[{"name":"Department of Structural Biology, The Weizmann Institute of Science, 7610001 Rehovot, Israel;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alicia","family":"Jimenez-Fernandez","sequence":"additional","affiliation":[{"name":"The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6705-3989","authenticated-orcid":false,"given":"Ruggero","family":"La Rosa","sequence":"additional","affiliation":[{"name":"The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800 Kgs. Lyngby, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rocio","family":"Espinosa Portero","sequence":"additional","affiliation":[{"name":"The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800 Kgs. 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Microbiol."},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev-biochem-062917-011942","article-title":"Ribosome-targeting antibiotics: Modes of action, mechanisms of resistance, and implications for drug design","volume":"87","author":"Lin J.","year":"2018","unstructured":"J. Lin, D. Zhou, T. A. Steitz, Y. S. Polikanov, M. G. Gagnon, Ribosome-targeting antibiotics: Modes of action, mechanisms of resistance, and implications for drug design. Annu. Rev. Biochem. 87, 451\u2013478 (2018).","journal-title":"Annu. Rev. Biochem."},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"2272","DOI":"10.1093\/emboj\/21.9.2272","article-title":"Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic","volume":"21","author":"Hirokawa G.","year":"2002","unstructured":"G. Hirokawa ., Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic. 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Biochem."},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"7896","DOI":"10.1038\/ncomms8896","article-title":"Chemically related 4,5-linked aminoglycoside antibiotics drive subunit rotation in opposite directions","volume":"6","author":"Wasserman M. R.","year":"2015","unstructured":"M. R. Wasserman ., Chemically related 4,5-linked aminoglycoside antibiotics drive subunit rotation in opposite directions. Nat. Commun. 6, 7896 (2015).","journal-title":"Nat. Commun."},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1039\/C5MD00344J","article-title":"Mechanisms of resistance to aminoglycoside antibiotics: Overview and perspectives","volume":"7","author":"Garneau-Tsodikova S.","year":"2016","unstructured":"S. Garneau-Tsodikova, K. J. Labby, Mechanisms of resistance to aminoglycoside antibiotics: Overview and perspectives. 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EMBO J. 18, 3133\u20133138 (1999).","journal-title":"EMBO J."},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1038\/nsmb.2360","article-title":"Allosteric control of the ribosome by small-molecule antibiotics","volume":"19","author":"Wang L.","year":"2012","unstructured":"L. Wang ., Allosteric control of the ribosome by small-molecule antibiotics. Nat. Struct. Mol. Biol. 19, 957\u2013963 (2012).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1128\/CMR.00117-14","article-title":"The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria","volume":"28","author":"Li X. Z.","year":"2015","unstructured":"X. Z. Li, P. Pl\u00e9siat, H. Nikaido, The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria. Clin. Microbiol. Rev. 28, 337\u2013418 (2015).","journal-title":"Clin. Microbiol. Rev."},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.drup.2010.08.003","article-title":"Aminoglycoside modifying enzymes","volume":"13","author":"Ramirez M. S.","year":"2010","unstructured":"M. S. Ramirez, M. E. Tolmasky, Aminoglycoside modifying enzymes. Drug Resist. Updat. 13, 151\u2013171 (2010).","journal-title":"Drug Resist. Updat."},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.drup.2012.05.001","article-title":"Exogenously acquired 16S rRNA methyltransferases found in aminoglycoside-resistant pathogenic gram-negative bacteria: An update","volume":"15","author":"Wachino J.","year":"2012","unstructured":"J. Wachino, Y. Arakawa, Exogenously acquired 16S rRNA methyltransferases found in aminoglycoside-resistant pathogenic gram-negative bacteria: An update. Drug Resist. Updat. 15, 133\u2013148 (2012).","journal-title":"Drug Resist. Updat."},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.sbi.2014.01.002","article-title":"A new system for naming ribosomal proteins","volume":"24","author":"Ban N.","year":"2014","unstructured":"N. Ban ., A new system for naming ribosomal proteins. Curr. Opin. Struct. Biol. 24, 165\u2013169 (2014).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"e_1_3_4_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/microbiolspec.VMBF-0016-2015"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1007\/BF00455118","article-title":"Alteration of ribosomal protein L6 in mutants of Escherichia coli resistant to gentamicin","volume":"158","author":"Buckel P.","year":"1977","unstructured":"P. Buckel, A. Buchberger, A. B\u00f6ck, H. G. Wittmann, Alteration of ribosomal protein L6 in mutants of Escherichia coli resistant to gentamicin. Mol. Gen. Genet. 158, 47\u201354 (1977).","journal-title":"Mol. Gen. Genet."},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1021\/bi00568a028","article-title":"Alteration of ribosomal protein L6 in gentamicin-resistant strains of Escherichia coli. Effects on fidelity of protein synthesis","volume":"18","author":"K\u00fchberger R.","year":"1979","unstructured":"R. K\u00fchberger, W. Piepersberg, A. Petzet, P. Buckel, A. B\u00f6ck, Alteration of ribosomal protein L6 in gentamicin-resistant strains of Escherichia coli. Effects on fidelity of protein synthesis. Biochemistry 18, 187\u2013193 (1979).","journal-title":"Biochemistry"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/j.jmb.2007.10.003","article-title":"Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome","volume":"374","author":"Sharma D.","year":"2007","unstructured":"D. Sharma, A. R. Cukras, E. J. Rogers, D. R. Southworth, R. Green, Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome. J. Mol. Biol. 374, 1065\u20131076 (2007).","journal-title":"J. Mol. Biol."},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/ng.3148","article-title":"Convergent evolution and adaptation of Pseudomonas aeruginosa within patients with cystic fibrosis","volume":"47","author":"Marvig R. L.","year":"2015","unstructured":"R. L. Marvig, L. M. Sommer, S. Molin, H. K. Johansen, Convergent evolution and adaptation of Pseudomonas aeruginosa within patients with cystic fibrosis. Nat. Genet. 47, 57\u201364 (2015).","journal-title":"Nat. Genet."},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"747","DOI":"10.15252\/msb.20145379","article-title":"Emergence of robust growth laws from optimal regulation of ribosome synthesis","volume":"10","author":"Scott M.","year":"2014","unstructured":"M. Scott, S. Klumpp, E. M. Mateescu, T. Hwa, Emergence of robust growth laws from optimal regulation of ribosome synthesis. Mol. Syst. Biol. 10, 747 (2014).","journal-title":"Mol. Syst. Biol."},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1126\/science.1060612","article-title":"Recognition of cognate transfer RNA by the 30S ribosomal subunit","volume":"292","author":"Ogle J. M.","year":"2001","unstructured":"J. M. Ogle ., Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292, 897\u2013902 (2001).","journal-title":"Science"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1038\/nature10913","article-title":"A new understanding of the decoding principle on the ribosome","volume":"484","author":"Demeshkina N.","year":"2012","unstructured":"N. Demeshkina, L. Jenner, E. Westhof, M. Yusupov, G. Yusupova, A new understanding of the decoding principle on the ribosome. 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Adv."},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"13359","DOI":"10.1073\/pnas.1810555115","article-title":"HflXr, a homolog of a ribosome-splitting factor, mediates antibiotic resistance","volume":"115","author":"Duval M.","year":"2018","unstructured":"M. Duval ., HflXr, a homolog of a ribosome-splitting factor, mediates antibiotic resistance. Proc. Natl. Acad. Sci. U.S.A. 115, 13359\u201313364 (2018).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"D666","DOI":"10.1093\/nar\/gks1119","article-title":"The standard European vector architecture (SEVA): A coherent platform for the analysis and deployment of complex prokaryotic phenotypes","volume":"41","author":"Silva-Rocha R.","year":"2013","unstructured":"R. Silva-Rocha ., The standard European vector architecture (SEVA): A coherent platform for the analysis and deployment of complex prokaryotic phenotypes. Nucleic Acids Res. 41, D666\u2013D675 (2013).","journal-title":"Nucleic Acids Res."},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/0076-6879(79)68019-9","article-title":"Plasmid cloning vehicles derived from plasmids ColE1, F, R6K, and RK2","volume":"68","author":"Kahn M.","year":"1979","unstructured":"M. Kahn ., Plasmid cloning vehicles derived from plasmids ColE1, F, R6K, and RK2. Methods Enzymol. 68, 268\u2013280 (1979).","journal-title":"Methods Enzymol"},{"key":"e_1_3_4_28_2","first-page":"931","volume-title":"Molecular Cloning: A Laboratory Manual","author":"Sambrook J.","year":"1989","unstructured":"J. Sambrook, E. F. Fritsch, T. Maniatis, Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989), pp. 931\u2013957."},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1128\/AAC.45.6.1900-1904.2001","article-title":"Staphylococcus aureus cell extract transcription-translation assay: Firefly luciferase reporter system for evaluating protein translation inhibitors","volume":"45","author":"Murray R. W.","year":"2001","unstructured":"R. W. Murray, E. P. Melchior, J. C. Hagadorn, K. R. Marotti, Staphylococcus aureus cell extract transcription-translation assay: Firefly luciferase reporter system for evaluating protein translation inhibitors. Antimicrob. Agents Chemother. 45, 1900\u20131904 (2001).","journal-title":"Antimicrob. Agents Chemother."},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"11460","DOI":"10.1038\/s41598-019-48019-1","article-title":"Exit tunnel modulation as resistance mechanism of S. aureus erythromycin resistant mutant","volume":"9","author":"Halfon Y.","year":"2019","unstructured":"Y. Halfon ., Exit tunnel modulation as resistance mechanism of S. aureus erythromycin resistant mutant. Sci. Rep. 9, 11460 (2019).","journal-title":"Sci. Rep."},{"key":"e_1_3_4_31_2","volume-title":"GraFit Version 7","author":"Leatherbarrow R. J.","year":"2010","unstructured":"R. J. Leatherbarrow, GraFit Version 7 (Erithacus Software Ltd., Horley, U.K., 2010)."},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.1038\/s41467-017-01664-4","article-title":"Atomic resolution snapshot of Leishmania ribosome inhibition by the aminoglycoside paromomycin","volume":"8","author":"Shalev-Benami M.","year":"2017","unstructured":"M. Shalev-Benami ., Atomic resolution snapshot of Leishmania ribosome inhibition by the aminoglycoside paromomycin. Nat. Commun. 8, 1589 (2017).","journal-title":"Nat. Commun."},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","unstructured":"S. Zheng E. Palovcak J.-P. Armache Y. Cheng D. Agard Anisotropic correction of beam-induced motion for improved single-particle electron cryo-microscopy. bioRxiv:10.1101\/061960 (4 July 2016).","DOI":"10.1101\/061960"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","unstructured":"A. Rohou N. Grigorieff CTFFIND4: Fast and accurate defocus estimation from electron micrographs. bioRxiv:10.1101\/020917 (13 August 2015).","DOI":"10.1101\/020917"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","article-title":"RELION: Implementation of a Bayesian approach to cryo-EM structure determination","volume":"180","author":"Scheres S. H.","year":"2012","unstructured":"S. H. Scheres, RELION: Implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519\u2013530 (2012).","journal-title":"J. Struct. Biol."},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/nmeth.2727","article-title":"Quantifying the local resolution of cryo-EM density maps","volume":"11","author":"Kucukelbir A.","year":"2014","unstructured":"A. Kucukelbir, F. J. Sigworth, H. D. Tagare, Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63\u201365 (2014).","journal-title":"Nat. Methods"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014A visualization system for exploratory research and analysis","volume":"25","author":"Pettersen E. F.","year":"2004","unstructured":"E. F. Pettersen ., UCSF Chimera\u2014A visualization system for exploratory research and analysis. J. Comput. 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