Open Access
Proceedings of the National Academy of Sciences of the United States of America, volume 107, issue 40, pages 17158-17163
Revisiting the structures of several antibiotics bound to the bacterial ribosome
1
Departments of Chemistry and
3
Howard Hughes Medical Institute, New Haven, CT 06511
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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:
20876130
Multidisciplinary
Abstract
The increasing prevalence of antibiotic-resistant pathogens reinforces the need for structures of antibiotic-ribosome complexes that are accurate enough to enable the rational design of novel ribosome-targeting therapeutics. Structures of many antibiotics in complex with both archaeal and eubacterial ribosomes have been determined, yet discrepancies between several of these models have raised the question of whether these differences arise from species-specific variations or from experimental problems. Our structure of chloramphenicol in complex with the 70S ribosome from Thermus thermophilus suggests a model for chloramphenicol bound to the large subunit of the bacterial ribosome that is radically different from the prevailing model. Further, our structures of the macrolide antibiotics erythromycin and azithromycin in complex with a bacterial ribosome are indistinguishable from those determined of complexes with the 50S subunit of Haloarcula marismortui, but differ significantly from the models that have been published for 50S subunit complexes of the eubacterium Deinococcus radiodurans. Our structure of the antibiotic telithromycin bound to the T. thermophilus ribosome reveals a lactone ring with a conformation similar to that observed in the H. marismortui and D. radiodurans complexes. However, the alkyl-aryl moiety is oriented differently in all three organisms, and the contacts observed with the T. thermophilus ribosome are consistent with biochemical studies performed on the Escherichia coli ribosome. Thus, our results support a mode of macrolide binding that is largely conserved across species, suggesting that the quality and interpretation of electron density, rather than species specificity, may be responsible for many of the discrepancies between the models.
Citations by journals
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Bulkley D. et al. Revisiting the structures of several antibiotics bound to the bacterial ribosome // Proceedings of the National Academy of Sciences of the United States of America. 2010. Vol. 107. No. 40. pp. 17158-17163.
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Bulkley D., Innis C. A., Blaha G., Steitz T. A. Revisiting the structures of several antibiotics bound to the bacterial ribosome // Proceedings of the National Academy of Sciences of the United States of America. 2010. Vol. 107. No. 40. pp. 17158-17163.
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TY - JOUR
DO - 10.1073/pnas.1008685107
UR - https://doi.org/10.1073%2Fpnas.1008685107
TI - Revisiting the structures of several antibiotics bound to the bacterial ribosome
T2 - Proceedings of the National Academy of Sciences of the United States of America
AU - Bulkley, David
AU - Innis, C Axel
AU - Blaha, Gregor
AU - Steitz, Thomas A.
PY - 2010
DA - 2010/09/27 00:00:00
PB - Proceedings of the National Academy of Sciences (PNAS)
SP - 17158-17163
IS - 40
VL - 107
PMID - 20876130
SN - 0027-8424
SN - 1091-6490
ER -
Cite this
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@article{2010_Bulkley,
author = {David Bulkley and C Axel Innis and Gregor Blaha and Thomas A. Steitz},
title = {Revisiting the structures of several antibiotics bound to the bacterial ribosome},
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.1008685107},
number = {40},
pages = {17158--17163},
doi = {10.1073/pnas.1008685107}
}
Cite this
MLA
Copy
Bulkley, David, et al. “Revisiting the structures of several antibiotics bound to the bacterial ribosome.” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 40, Sep. 2010, pp. 17158-17163. https://doi.org/10.1073%2Fpnas.1008685107.