Open Access
Proceedings of the National Academy of Sciences of the United States of America, volume 107, issue 40, pages 17152-17157
Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action
1
Departments of Molecular and Cell Biology and Chemistry, University of California, Berkeley, CA 94720;
2
Center for Pharmaceutical Biotechnology, University of Illinois, Chicago, IL 60607; and
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Publication type: Journal Article
Publication date: 2010-09-27
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 11.1
ISSN: 00278424, 10916490
PubMed ID:
20876128
Multidisciplinary
Abstract
Differences between the structures of bacterial, archaeal, and eukaryotic ribosomes account for the selective action of antibiotics. Even minor variations in the structure of ribosomes of different bacterial species may lead to idiosyncratic, species-specific interactions of the drugs with their targets. Although crystallographic structures of antibiotics bound to the peptidyl transferase center or the exit tunnel of archaeal (Haloarcula marismortui) and bacterial (Deinococcus radiodurans) large ribosomal subunits have been reported, it remains unclear whether the interactions of antibiotics with these ribosomes accurately reflect those with the ribosomes of pathogenic bacteria. Here we report X-ray crystal structures of the Escherichia coli ribosome in complexes with clinically important antibiotics of four major classes, including the macrolide erythromycin, the ketolide telithromycin, the lincosamide clindamycin, and a phenicol, chloramphenicol, at resolutions of ∼3.3 Å–3.4 Å. Binding modes of three of these antibiotics show important variations compared to the previously determined structures. Biochemical and structural evidence also indicates that interactions of telithromycin with the E. coli ribosome more closely resembles drug binding to ribosomes of bacterial pathogens. The present data further argue that the identity of nucleotides 752, 2609, and 2055 of 23S ribosomal RNA explain in part the spectrum and selectivity of antibiotic action.
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Dunkle J. A. et al. Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action // Proceedings of the National Academy of Sciences of the United States of America. 2010. Vol. 107. No. 40. pp. 17152-17157.
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Dunkle J. A., Xiong L., Mankin A. S., Cate J. H. D. Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action // Proceedings of the National Academy of Sciences of the United States of America. 2010. Vol. 107. No. 40. pp. 17152-17157.
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TY - JOUR
DO - 10.1073/pnas.1007988107
UR - https://doi.org/10.1073%2Fpnas.1007988107
TI - Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action
T2 - Proceedings of the National Academy of Sciences of the United States of America
AU - Dunkle, Jack A.
AU - Xiong, Liqun
AU - Mankin, Alexander S
AU - Cate, Jamie H. D.
PY - 2010
DA - 2010/09/27 00:00:00
PB - Proceedings of the National Academy of Sciences (PNAS)
SP - 17152-17157
IS - 40
VL - 107
PMID - 20876128
SN - 0027-8424
SN - 1091-6490
ER -
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@article{2010_Dunkle,
author = {Jack A. Dunkle and Liqun Xiong and Alexander S Mankin and Jamie H. D. Cate},
title = {Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {2010},
volume = {107},
publisher = {Proceedings of the National Academy of Sciences (PNAS)},
month = {sep},
url = {https://doi.org/10.1073%2Fpnas.1007988107},
number = {40},
pages = {17152--17157},
doi = {10.1073/pnas.1007988107}
}
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MLA
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Dunkle, Jack A., et al. “Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action.” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 40, Sep. 2010, pp. 17152-17157. https://doi.org/10.1073%2Fpnas.1007988107.