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Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase
Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec prot...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4252904/ https://www.ncbi.nlm.nih.gov/pubmed/25466392 http://dx.doi.org/10.1038/srep07299 |
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author | Kumazaki, Kaoru Kishimoto, Toshiki Furukawa, Arata Mori, Hiroyuki Tanaka, Yoshiki Dohmae, Naoshi Ishitani, Ryuichiro Tsukazaki, Tomoya Nureki, Osamu |
author_facet | Kumazaki, Kaoru Kishimoto, Toshiki Furukawa, Arata Mori, Hiroyuki Tanaka, Yoshiki Dohmae, Naoshi Ishitani, Ryuichiro Tsukazaki, Tomoya Nureki, Osamu |
author_sort | Kumazaki, Kaoru |
collection | PubMed |
description | Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec proteins, forming a multi-protein complex for Sec-dependent membrane protein integration. Here, we report the crystal structure of full-length Escherichia coli YidC. The structure reveals that a hydrophilic groove, formed by five transmembrane helices, is a conserved structural feature of YidC, as compared to the previous YidC structure from Bacillus halodurans, which lacks a periplasmic domain. Structural mapping of the substrate- or Sec protein-contact sites suggested the importance of the groove for the YidC functions as a chaperone and an insertase, and provided structural insight into the multi-protein complex. |
format | Online Article Text |
id | pubmed-4252904 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-42529042014-12-08 Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase Kumazaki, Kaoru Kishimoto, Toshiki Furukawa, Arata Mori, Hiroyuki Tanaka, Yoshiki Dohmae, Naoshi Ishitani, Ryuichiro Tsukazaki, Tomoya Nureki, Osamu Sci Rep Article Bacterial YidC, an evolutionally conserved membrane protein, functions as a membrane protein chaperone in cooperation with the Sec translocon and as an independent insertase for membrane proteins. In Gram-negative bacteria, the transmembrane and periplasmic regions of YidC interact with the Sec proteins, forming a multi-protein complex for Sec-dependent membrane protein integration. Here, we report the crystal structure of full-length Escherichia coli YidC. The structure reveals that a hydrophilic groove, formed by five transmembrane helices, is a conserved structural feature of YidC, as compared to the previous YidC structure from Bacillus halodurans, which lacks a periplasmic domain. Structural mapping of the substrate- or Sec protein-contact sites suggested the importance of the groove for the YidC functions as a chaperone and an insertase, and provided structural insight into the multi-protein complex. Nature Publishing Group 2014-12-03 /pmc/articles/PMC4252904/ /pubmed/25466392 http://dx.doi.org/10.1038/srep07299 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/ |
spellingShingle | Article Kumazaki, Kaoru Kishimoto, Toshiki Furukawa, Arata Mori, Hiroyuki Tanaka, Yoshiki Dohmae, Naoshi Ishitani, Ryuichiro Tsukazaki, Tomoya Nureki, Osamu Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase |
title | Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase |
title_full | Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase |
title_fullStr | Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase |
title_full_unstemmed | Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase |
title_short | Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase |
title_sort | crystal structure of escherichia coli yidc, a membrane protein chaperone and insertase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4252904/ https://www.ncbi.nlm.nih.gov/pubmed/25466392 http://dx.doi.org/10.1038/srep07299 |
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