Open Access
RNA, volume 25, issue 5, pages 600-606
High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition
Publication type: Journal Article
Publication date: 2019-02-07
PubMed ID:
30733327
Molecular Biology
Abstract
The 70S ribosome is a major target for antibacterial drugs. Two of the classical antibiotics, chloramphenicol (CHL) and erythromycin (ERY), competitively bind to adjacent but separate sites on the bacterial ribosome: the catalytic peptidyl transferase center (PTC) and the nascent polypeptide exit tunnel (NPET), respectively. The previously reported competitive binding of CHL and ERY might be due either to a direct collision of the two drugs on the ribosome or due to a drug-induced allosteric effect. Because of the resolution limitations, the available structures of these antibiotics in complex with bacterial ribosomes do not allow us to discriminate between these two possible mechanisms. In this work, we have obtained two crystal structures of CHL and ERY in complex with the Thermus thermophilus 70S ribosome at a higher resolution (2.65 and 2.89 Å, respectively) allowing unambiguous placement of the drugs in the electron density maps. Our structures provide evidence of the direct collision of CHL and ERY on the ribosome, which rationalizes the observed competition between the two drugs.
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Citations by publishers
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1 publication, 2.13%
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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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Svetlov M. S. et al. High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition // RNA. 2019. Vol. 25. No. 5. pp. 600-606.
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Svetlov M. S., Plessa E., Chen C. W., Bougas A., Krokidis M. G., Dinos G. P., Polikanov Y. S. High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition // RNA. 2019. Vol. 25. No. 5. pp. 600-606.
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TY - JOUR
DO - 10.1261/rna.069260.118
UR - https://doi.org/10.1261%2Frna.069260.118
TI - High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition
T2 - RNA
AU - Svetlov, Maxim S
AU - Plessa, Elena
AU - Chen, Chih Wei
AU - Bougas, Anthony
AU - Krokidis, Marios G
AU - Dinos, George P.
AU - Polikanov, Yury S
PY - 2019
DA - 2019/02/07 00:00:00
PB - Cold Spring Harbor Laboratory
SP - 600-606
IS - 5
VL - 25
PMID - 30733327
SN - 1355-8382
SN - 1469-9001
ER -
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@article{2019_Svetlov
author = {Maxim S Svetlov and Elena Plessa and Chih Wei Chen and Anthony Bougas and Marios G Krokidis and George P. Dinos and Yury S Polikanov},
title = {High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition},
journal = {RNA},
year = {2019},
volume = {25},
publisher = {Cold Spring Harbor Laboratory},
month = {feb},
url = {https://doi.org/10.1261%2Frna.069260.118},
number = {5},
pages = {600--606},
doi = {10.1261/rna.069260.118}
}
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MLA
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Svetlov, Maxim S., et al. “High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition.” RNA, vol. 25, no. 5, Feb. 2019, pp. 600-606. https://doi.org/10.1261%2Frna.069260.118.