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Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System
The type VI secretion system (T6SS) is a bacterial macromolecular machine widely distributed in Gram-negative bacteria, which transports effector proteins into eukaryotic host cells or other bacteria. Membrane complexes and a central tubular structure, which resembles the tail of contractile bacteri...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4469607/ https://www.ncbi.nlm.nih.gov/pubmed/26079269 http://dx.doi.org/10.1371/journal.pone.0129691 |
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author | Ruiz, Federico M. Santillana, Elena Spínola-Amilibia, Mercedes Torreira, Eva Culebras, Esther Romero, Antonio |
author_facet | Ruiz, Federico M. Santillana, Elena Spínola-Amilibia, Mercedes Torreira, Eva Culebras, Esther Romero, Antonio |
author_sort | Ruiz, Federico M. |
collection | PubMed |
description | The type VI secretion system (T6SS) is a bacterial macromolecular machine widely distributed in Gram-negative bacteria, which transports effector proteins into eukaryotic host cells or other bacteria. Membrane complexes and a central tubular structure, which resembles the tail of contractile bacteriophages, compose the T6SS. One of the proteins forming this tube is the hemolysin co-regulated protein (Hcp), which acts as virulence factor, as transporter of effectors and as a chaperone. In this study, we present the structure of Hcp from Acinetobacter baumannii, together with functional and oligomerization studies. The structure of this protein exhibits a tight β barrel formed by two β sheets and flanked at one side by a short α-helix. Six Hcp molecules associate to form a donut-shaped hexamer, as observed in both the crystal structure and solution. These results emphasize the importance of this oligomerization state in this family of proteins, despite the low similarity of sequence among them. The structure presented in this study is the first one for a protein forming part of a functional T6SS from A. baumannii. These results will help us to understand the mechanism and function of this secretion system in this opportunistic nosocomial pathogen. |
format | Online Article Text |
id | pubmed-4469607 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-44696072015-06-22 Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System Ruiz, Federico M. Santillana, Elena Spínola-Amilibia, Mercedes Torreira, Eva Culebras, Esther Romero, Antonio PLoS One Research Article The type VI secretion system (T6SS) is a bacterial macromolecular machine widely distributed in Gram-negative bacteria, which transports effector proteins into eukaryotic host cells or other bacteria. Membrane complexes and a central tubular structure, which resembles the tail of contractile bacteriophages, compose the T6SS. One of the proteins forming this tube is the hemolysin co-regulated protein (Hcp), which acts as virulence factor, as transporter of effectors and as a chaperone. In this study, we present the structure of Hcp from Acinetobacter baumannii, together with functional and oligomerization studies. The structure of this protein exhibits a tight β barrel formed by two β sheets and flanked at one side by a short α-helix. Six Hcp molecules associate to form a donut-shaped hexamer, as observed in both the crystal structure and solution. These results emphasize the importance of this oligomerization state in this family of proteins, despite the low similarity of sequence among them. The structure presented in this study is the first one for a protein forming part of a functional T6SS from A. baumannii. These results will help us to understand the mechanism and function of this secretion system in this opportunistic nosocomial pathogen. Public Library of Science 2015-06-16 /pmc/articles/PMC4469607/ /pubmed/26079269 http://dx.doi.org/10.1371/journal.pone.0129691 Text en © 2015 Ruiz et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ruiz, Federico M. Santillana, Elena Spínola-Amilibia, Mercedes Torreira, Eva Culebras, Esther Romero, Antonio Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System |
title | Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System |
title_full | Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System |
title_fullStr | Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System |
title_full_unstemmed | Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System |
title_short | Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System |
title_sort | crystal structure of hcp from acinetobacter baumannii: a component of the type vi secretion system |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4469607/ https://www.ncbi.nlm.nih.gov/pubmed/26079269 http://dx.doi.org/10.1371/journal.pone.0129691 |
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