Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System
| العنوان: | Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System |
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| المؤلفون: | Esther Culebras, Eva Torreira, Federico M. Ruiz, Mercedes Spínola-Amilibia, Antonio A. Romero, Elena Santillana |
| المصدر: | PLoS ONE PLoS ONE, Vol 10, Iss 6, p e0129691 (2015) Digital.CSIC. Repositorio Institucional del CSIC instname Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid Consejería de Sanidad de la Comunidad de Madrid |
| بيانات النشر: | Public Library of Science, 2015. |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | Acinetobacter baumannii, Models, Molecular, lcsh:Medicine, Random hexamer, Crystallography, X-Ray, Virulence factor, Protein Structure, Secondary, Microbiology, Protein structure, Bacterial Proteins, Secretion, Protein Structure, Quaternary, lcsh:Science, Type VI secretion system, Multidisciplinary, biology, Chemistry, Effector, lcsh:R, Correction, Type VI Secretion Systems, biology.organism_classification, Chaperone (protein), biology.protein, Biophysics, lcsh:Q, Protein Multimerization, Research Article |
| الوصف: | 16 p.-6 fig.-1 tab. 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. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 1932-6203 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e832c866ee97c2c473f3f6b3c3a4ec7f http://europepmc.org/articles/PMC4469607 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....e832c866ee97c2c473f3f6b3c3a4ec7f |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19326203 |
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