Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Macé, Kevin, Giudice, Emmanuel, Chat, Sophie, Gillet, Reynald
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
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
_version_ 1783312339278233600
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
work_keys_str_mv AT macekevin thestructureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors
AT giudiceemmanuel thestructureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors
AT chatsophie thestructureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors
AT gilletreynald thestructureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors
AT macekevin structureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors
AT giudiceemmanuel structureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors
AT chatsophie structureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors
AT gilletreynald structureofanelongationfactorgribosomecomplexcapturedintheabsenceofinhibitors