Carter, Andrew P. and Clemons, William M. and Brodersen, Ditlev E. and Morgan-Warren, Robert J. and Wimberly, Brian T. and Ramakrishnan, V. (2000) Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature, 407 (6802). pp. 340-348. ISSN 0028-0836. doi:10.1038/35030019. https://resolver.caltech.edu/CaltechAUTHORS:20181030-134119194
![]() |
Video (QuickTime)
- Supplemental Material
See Usage Policy. 6MB |
![]() |
Image (JPEG) (Annotated figure (front))
- Supplemental Material
See Usage Policy. 165kB |
![]() |
Image (JPEG) (Annotated figure (back))
- Supplemental Material
See Usage Policy. 162kB |
![]() |
MS Word (Table 1)
- Supplemental Material
See Usage Policy. 26kB |
Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20181030-134119194
Abstract
The 30S ribosomal subunit has two primary functions in protein synthesis. It discriminates against aminoacyl transfer RNAs that do not match the codon of messenger RNA, thereby ensuring accuracy in translation of the genetic message in a process called decoding. Also, it works with the 50S subunit to move the tRNAs and associated mRNA by precisely one codon, in a process called translocation. Here we describe the functional implications of the high-resolution 30S crystal structure presented in the accompanying paper, and infer details of the interactions between the 30S subunit and its tRNA and mRNA ligands. We also describe the crystal structure of the 30S subunit complexed with the antibiotics paromomycin, streptomycin and spectinomycin, which interfere with decoding and translocation. This work reveals the structural basis for the action of these antibiotics, and leads to a model for the role of the universally conserved 16S RNA residues A1492 and A1493 in the decoding process.
Item Type: | Article | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Related URLs: |
| |||||||||
ORCID: |
| |||||||||
Additional Information: | © 2000 Nature Publishing Group. Received 14 July; accepted 10 August 2000. This work was supported by the Medical Research Council (UK) and a grant from the US National Institutes of Health to V.R. and S.W.White. D.E.B. was supported by an EMBO long-term fellowship, and W.M.C. by an NIH predoctoral fellowship. We thank R. Ravelli for help with data collection, and M. Pacold for help and discussions with the modelling of antibiotic structures. Andrew P. Carter, William M. Clemons & Ditlev E. Brodersen -- These authors contributed equally to this work. | |||||||||
Funders: |
| |||||||||
Issue or Number: | 6802 | |||||||||
DOI: | 10.1038/35030019 | |||||||||
Record Number: | CaltechAUTHORS:20181030-134119194 | |||||||||
Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20181030-134119194 | |||||||||
Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | |||||||||
ID Code: | 90509 | |||||||||
Collection: | CaltechAUTHORS | |||||||||
Deposited By: | George Porter | |||||||||
Deposited On: | 31 Oct 2018 14:08 | |||||||||
Last Modified: | 16 Nov 2021 03:33 |
Repository Staff Only: item control page