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The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors
During translation’s elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G–ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydroly...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5887593/ https://www.ncbi.nlm.nih.gov/pubmed/29408956 http://dx.doi.org/10.1093/nar/gky081 |
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author | Macé, Kevin Giudice, Emmanuel Chat, Sophie Gillet, Reynald |
author_facet | Macé, Kevin Giudice, Emmanuel Chat, Sophie Gillet, Reynald |
author_sort | Macé, Kevin |
collection | PubMed |
description | During translation’s elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G–ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydrolyzable guanosine 5′-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G form. Here, we present the first cryo-electron microscopy structure of EF-G bound to ribosome in the absence of an inhibitor. The structure reveals a natural conformation of EF-G·GDP in the ribosome, with a previously unseen conformation of its third domain. These data show how EF-G must affect translocation, and suggest the molecular mechanism by which fusidic acid antibiotic prevents the release of EF-G after GTP hydrolysis. |
format | Online Article Text |
id | pubmed-5887593 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-58875932018-04-11 The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors Macé, Kevin Giudice, Emmanuel Chat, Sophie Gillet, Reynald Nucleic Acids Res Structural Biology During translation’s elongation cycle, elongation factor G (EF-G) promotes messenger and transfer RNA translocation through the ribosome. Until now, the structures reported for EF-G–ribosome complexes have been obtained by trapping EF-G in the ribosome. These results were based on use of non-hydrolyzable guanosine 5′-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G form. Here, we present the first cryo-electron microscopy structure of EF-G bound to ribosome in the absence of an inhibitor. The structure reveals a natural conformation of EF-G·GDP in the ribosome, with a previously unseen conformation of its third domain. These data show how EF-G must affect translocation, and suggest the molecular mechanism by which fusidic acid antibiotic prevents the release of EF-G after GTP hydrolysis. Oxford University Press 2018-04-06 2018-02-02 /pmc/articles/PMC5887593/ /pubmed/29408956 http://dx.doi.org/10.1093/nar/gky081 Text en © The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Structural Biology Macé, Kevin Giudice, Emmanuel Chat, Sophie Gillet, Reynald The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors |
title | The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors |
title_full | The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors |
title_fullStr | The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors |
title_full_unstemmed | The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors |
title_short | The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors |
title_sort | structure of an elongation factor g-ribosome complex captured in the absence of inhibitors |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5887593/ https://www.ncbi.nlm.nih.gov/pubmed/29408956 http://dx.doi.org/10.1093/nar/gky081 |
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