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Large conformational changes of a highly dynamic pre-protein binding domain in SecA
SecA is an essential molecular motor for the translocation of proteins across the membrane via the bacterial Sec secretion system. While the Sec system is found in all cells from archaea to multicellular eukaryotes, the SecA protein is mainly found in bacteria. The mechanism of how the motor protein...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6123708/ https://www.ncbi.nlm.nih.gov/pubmed/30272009 http://dx.doi.org/10.1038/s42003-018-0133-4 |
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author | Ernst, Isabel Haase, Maximilian Ernst, Stefan Yuan, Shuguang Kuhn, Andreas Leptihn, Sebastian |
author_facet | Ernst, Isabel Haase, Maximilian Ernst, Stefan Yuan, Shuguang Kuhn, Andreas Leptihn, Sebastian |
author_sort | Ernst, Isabel |
collection | PubMed |
description | SecA is an essential molecular motor for the translocation of proteins across the membrane via the bacterial Sec secretion system. While the Sec system is found in all cells from archaea to multicellular eukaryotes, the SecA protein is mainly found in bacteria. The mechanism of how the motor protein works on a molecular level is still under dispute but it is well established that SecA binds ATP and uses its hydrolysis for the translocation of substrates. In this work, we addressed the question of which conformational changes the protein might undergo during protein translocation. To this end, we investigated the molecular movements of SecA in the absence or the presence of ATP using single-molecule FRET measurements and in silico normal mode analyses. Our results demonstrate that the pre-protein binding domain of SecA is highly dynamic in the absence of the nucleotide and moves towards the helical wing domain in an ATP-bound state. |
format | Online Article Text |
id | pubmed-6123708 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61237082018-09-28 Large conformational changes of a highly dynamic pre-protein binding domain in SecA Ernst, Isabel Haase, Maximilian Ernst, Stefan Yuan, Shuguang Kuhn, Andreas Leptihn, Sebastian Commun Biol Article SecA is an essential molecular motor for the translocation of proteins across the membrane via the bacterial Sec secretion system. While the Sec system is found in all cells from archaea to multicellular eukaryotes, the SecA protein is mainly found in bacteria. The mechanism of how the motor protein works on a molecular level is still under dispute but it is well established that SecA binds ATP and uses its hydrolysis for the translocation of substrates. In this work, we addressed the question of which conformational changes the protein might undergo during protein translocation. To this end, we investigated the molecular movements of SecA in the absence or the presence of ATP using single-molecule FRET measurements and in silico normal mode analyses. Our results demonstrate that the pre-protein binding domain of SecA is highly dynamic in the absence of the nucleotide and moves towards the helical wing domain in an ATP-bound state. Nature Publishing Group UK 2018-09-03 /pmc/articles/PMC6123708/ /pubmed/30272009 http://dx.doi.org/10.1038/s42003-018-0133-4 Text en © The Author(s) 2018 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/. |
spellingShingle | Article Ernst, Isabel Haase, Maximilian Ernst, Stefan Yuan, Shuguang Kuhn, Andreas Leptihn, Sebastian Large conformational changes of a highly dynamic pre-protein binding domain in SecA |
title | Large conformational changes of a highly dynamic pre-protein binding domain in SecA |
title_full | Large conformational changes of a highly dynamic pre-protein binding domain in SecA |
title_fullStr | Large conformational changes of a highly dynamic pre-protein binding domain in SecA |
title_full_unstemmed | Large conformational changes of a highly dynamic pre-protein binding domain in SecA |
title_short | Large conformational changes of a highly dynamic pre-protein binding domain in SecA |
title_sort | large conformational changes of a highly dynamic pre-protein binding domain in seca |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6123708/ https://www.ncbi.nlm.nih.gov/pubmed/30272009 http://dx.doi.org/10.1038/s42003-018-0133-4 |
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