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Crystal structure of bacterial haem importer complex in the inward-facing conformation
Pathogenic bacteria remove iron from the haem of host tissues and use it as a catalytic center of many enzymes. Haem uptake by pathogenic bacteria is facilitated by the membrane-integrated haem importer, which belongs to the type II ATP-binding cassette (ABC) transporter. Here we present crystal str...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5136619/ https://www.ncbi.nlm.nih.gov/pubmed/27830695 http://dx.doi.org/10.1038/ncomms13411 |
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author | Naoe, Youichi Nakamura, Nozomi Doi, Akihiro Sawabe, Mia Nakamura, Hiro Shiro, Yoshitsugu Sugimoto, Hiroshi |
author_facet | Naoe, Youichi Nakamura, Nozomi Doi, Akihiro Sawabe, Mia Nakamura, Hiro Shiro, Yoshitsugu Sugimoto, Hiroshi |
author_sort | Naoe, Youichi |
collection | PubMed |
description | Pathogenic bacteria remove iron from the haem of host tissues and use it as a catalytic center of many enzymes. Haem uptake by pathogenic bacteria is facilitated by the membrane-integrated haem importer, which belongs to the type II ATP-binding cassette (ABC) transporter. Here we present crystal structures of Burkholderia cenocepacia haem importer BhuUV complexed with the periplasmic haem-binding protein BhuT and in the absence of BhuT. The transmembrane helices of these structures show an inward-facing conformation, in which the cytoplasmic gate of the haem translocation pathway is completely open. Since this conformation is found in both the haem- and nucleotide-free form, the structure of BhuUV-T provides the post-translocation state and the missing piece in the transport cycle of the type II importer. Structural comparison with the outward-facing conformation reported for the haem importer ortholog HmuUV from Yersenia pestis gives mechanistic insights into conformational transitions and haem secretion during the haem transport cycle. |
format | Online Article Text |
id | pubmed-5136619 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-51366192016-12-16 Crystal structure of bacterial haem importer complex in the inward-facing conformation Naoe, Youichi Nakamura, Nozomi Doi, Akihiro Sawabe, Mia Nakamura, Hiro Shiro, Yoshitsugu Sugimoto, Hiroshi Nat Commun Article Pathogenic bacteria remove iron from the haem of host tissues and use it as a catalytic center of many enzymes. Haem uptake by pathogenic bacteria is facilitated by the membrane-integrated haem importer, which belongs to the type II ATP-binding cassette (ABC) transporter. Here we present crystal structures of Burkholderia cenocepacia haem importer BhuUV complexed with the periplasmic haem-binding protein BhuT and in the absence of BhuT. The transmembrane helices of these structures show an inward-facing conformation, in which the cytoplasmic gate of the haem translocation pathway is completely open. Since this conformation is found in both the haem- and nucleotide-free form, the structure of BhuUV-T provides the post-translocation state and the missing piece in the transport cycle of the type II importer. Structural comparison with the outward-facing conformation reported for the haem importer ortholog HmuUV from Yersenia pestis gives mechanistic insights into conformational transitions and haem secretion during the haem transport cycle. Nature Publishing Group 2016-11-10 /pmc/articles/PMC5136619/ /pubmed/27830695 http://dx.doi.org/10.1038/ncomms13411 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 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 to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Naoe, Youichi Nakamura, Nozomi Doi, Akihiro Sawabe, Mia Nakamura, Hiro Shiro, Yoshitsugu Sugimoto, Hiroshi Crystal structure of bacterial haem importer complex in the inward-facing conformation |
title | Crystal structure of bacterial haem importer complex in the inward-facing conformation |
title_full | Crystal structure of bacterial haem importer complex in the inward-facing conformation |
title_fullStr | Crystal structure of bacterial haem importer complex in the inward-facing conformation |
title_full_unstemmed | Crystal structure of bacterial haem importer complex in the inward-facing conformation |
title_short | Crystal structure of bacterial haem importer complex in the inward-facing conformation |
title_sort | crystal structure of bacterial haem importer complex in the inward-facing conformation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5136619/ https://www.ncbi.nlm.nih.gov/pubmed/27830695 http://dx.doi.org/10.1038/ncomms13411 |
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