High-resolution structure of the Escherichia coli ribosome
Abstract
Protein synthesis by the ribosome is highly dependent on the ionic conditions in the cellular environment, but the roles of ribosome solvation remain poorly understood. Moreover, the function of modifications to ribosomal RNA and ribosomal proteins are unclear. Here we present the structure of the Escherichia coli 70S ribosome to 2.4 Å resolution. The structure reveals details of the ribosomal subunit interface that are conserved in all domains of life, and suggest how solvation contributes to ribosome integrity and function. The structure also suggests how the conformation of ribosomal protein uS12 likely impacts its contribution to messenger RNA decoding. In conclusion, this structure helps to explain the phylogenetic conservation of key elements of the ribosome, including posttranscriptional and posttranslational modifications and should serve as a basis for future antibiotic development.
- Authors:
-
- Univ. of California, Berkeley, CA (United States)
- Weill Cornell Medical College, New York, NY (United States)
- Weill Cornell Medical College, New York, NY (United States); Rockefeller Univ., New York, NY (United States)
- Publication Date:
- Research Org.:
- Univ. of California, Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1347117
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Journal Article: Accepted Manuscript
- Journal Name:
- Nature Structural & Molecular Biology
- Additional Journal Information:
- Journal Volume: 22; Journal Issue: 4; Journal ID: ISSN 1545-9993
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; drug recovery; evolution; single-molecule biophysics; X-ray crystallography
Citation Formats
Noeske, Jonas, Wasserman, Michael R., Terry, Daniel S., Altman, Roger B., Blanchard, Scott C., and Cate, Jamie H. D. High-resolution structure of the Escherichia coli ribosome. United States: N. p., 2015.
Web. doi:10.1038/nsmb.2994.
Noeske, Jonas, Wasserman, Michael R., Terry, Daniel S., Altman, Roger B., Blanchard, Scott C., & Cate, Jamie H. D. High-resolution structure of the Escherichia coli ribosome. United States. https://doi.org/10.1038/nsmb.2994
Noeske, Jonas, Wasserman, Michael R., Terry, Daniel S., Altman, Roger B., Blanchard, Scott C., and Cate, Jamie H. D. 2015.
"High-resolution structure of the Escherichia coli ribosome". United States. https://doi.org/10.1038/nsmb.2994. https://www.osti.gov/servlets/purl/1347117.
@article{osti_1347117,
title = {High-resolution structure of the Escherichia coli ribosome},
author = {Noeske, Jonas and Wasserman, Michael R. and Terry, Daniel S. and Altman, Roger B. and Blanchard, Scott C. and Cate, Jamie H. D.},
abstractNote = {Protein synthesis by the ribosome is highly dependent on the ionic conditions in the cellular environment, but the roles of ribosome solvation remain poorly understood. Moreover, the function of modifications to ribosomal RNA and ribosomal proteins are unclear. Here we present the structure of the Escherichia coli 70S ribosome to 2.4 Å resolution. The structure reveals details of the ribosomal subunit interface that are conserved in all domains of life, and suggest how solvation contributes to ribosome integrity and function. The structure also suggests how the conformation of ribosomal protein uS12 likely impacts its contribution to messenger RNA decoding. In conclusion, this structure helps to explain the phylogenetic conservation of key elements of the ribosome, including posttranscriptional and posttranslational modifications and should serve as a basis for future antibiotic development.},
doi = {10.1038/nsmb.2994},
url = {https://www.osti.gov/biblio/1347117},
journal = {Nature Structural & Molecular Biology},
issn = {1545-9993},
number = 4,
volume = 22,
place = {United States},
year = {Mon Mar 16 00:00:00 EDT 2015},
month = {Mon Mar 16 00:00:00 EDT 2015}
}
Web of Science
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Structure of the 70S ribosome from human pathogen Staphylococcus aureus
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Biogenesis and iron-dependency of ribosomal RNA hydroxylation
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Ribosomal Antibiotics: Contemporary Challenges
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