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The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services
Our understanding of protein synthesis has been conceptualised around the structure and function of the bacterial ribosome. This complex macromolecular machine is the target of important antimicrobial drugs, an integral line of defence against infectious diseases. Here, we describe how open access t...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9968351/ https://www.ncbi.nlm.nih.gov/pubmed/36841832 http://dx.doi.org/10.1038/s41467-023-36742-3 |
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author | Fromm, Simon A. O’Connor, Kate M. Purdy, Michael Bhatt, Pramod R. Loughran, Gary Atkins, John F. Jomaa, Ahmad Mattei, Simone |
author_facet | Fromm, Simon A. O’Connor, Kate M. Purdy, Michael Bhatt, Pramod R. Loughran, Gary Atkins, John F. Jomaa, Ahmad Mattei, Simone |
author_sort | Fromm, Simon A. |
collection | PubMed |
description | Our understanding of protein synthesis has been conceptualised around the structure and function of the bacterial ribosome. This complex macromolecular machine is the target of important antimicrobial drugs, an integral line of defence against infectious diseases. Here, we describe how open access to cryo-electron microscopy facilities combined with bespoke user support enabled structural determination of the translating ribosome from Escherichia coli at 1.55 Å resolution. The obtained structures allow for direct determination of the rRNA sequence to identify ribosome polymorphism sites in the E. coli strain used in this study and enable interpretation of the ribosomal active and peripheral sites at unprecedented resolution. This includes scarcely populated chimeric hybrid states of the ribosome engaged in several tRNA translocation steps resolved at ~2 Å resolution. The current map not only improves our understanding of protein synthesis but also allows for more precise structure-based drug design of antibiotics to tackle rising bacterial resistance. |
format | Online Article Text |
id | pubmed-9968351 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-99683512023-02-27 The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services Fromm, Simon A. O’Connor, Kate M. Purdy, Michael Bhatt, Pramod R. Loughran, Gary Atkins, John F. Jomaa, Ahmad Mattei, Simone Nat Commun Article Our understanding of protein synthesis has been conceptualised around the structure and function of the bacterial ribosome. This complex macromolecular machine is the target of important antimicrobial drugs, an integral line of defence against infectious diseases. Here, we describe how open access to cryo-electron microscopy facilities combined with bespoke user support enabled structural determination of the translating ribosome from Escherichia coli at 1.55 Å resolution. The obtained structures allow for direct determination of the rRNA sequence to identify ribosome polymorphism sites in the E. coli strain used in this study and enable interpretation of the ribosomal active and peripheral sites at unprecedented resolution. This includes scarcely populated chimeric hybrid states of the ribosome engaged in several tRNA translocation steps resolved at ~2 Å resolution. The current map not only improves our understanding of protein synthesis but also allows for more precise structure-based drug design of antibiotics to tackle rising bacterial resistance. Nature Publishing Group UK 2023-02-25 /pmc/articles/PMC9968351/ /pubmed/36841832 http://dx.doi.org/10.1038/s41467-023-36742-3 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Fromm, Simon A. O’Connor, Kate M. Purdy, Michael Bhatt, Pramod R. Loughran, Gary Atkins, John F. Jomaa, Ahmad Mattei, Simone The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services |
title | The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services |
title_full | The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services |
title_fullStr | The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services |
title_full_unstemmed | The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services |
title_short | The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services |
title_sort | translating bacterial ribosome at 1.55 å resolution generated by cryo-em imaging services |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9968351/ https://www.ncbi.nlm.nih.gov/pubmed/36841832 http://dx.doi.org/10.1038/s41467-023-36742-3 |
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