Structure of a type IV pilus machinery in the open and closed state

Proteins of the secretin family form large macromolecular complexes, which assemble in the outer membrane of Gram-negative bacteria. Secretins are major components of type II and III secretion systems and are linked to extrusion of type IV pili (T4P) and to DNA uptake. By electron cryo-tomography of...

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Autores principales: Gold, Vicki AM, Salzer, Ralf, Averhoff, Beate, Kühlbrandt, Werner
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2015
Materias:
Biophysics and Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4463427/
https://www.ncbi.nlm.nih.gov/pubmed/25997099
http://dx.doi.org/10.7554/eLife.07380
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author Gold, Vicki AM
Salzer, Ralf
Averhoff, Beate
Kühlbrandt, Werner
author_facet Gold, Vicki AM
Salzer, Ralf
Averhoff, Beate
Kühlbrandt, Werner
author_sort Gold, Vicki AM
collection PubMed
description Proteins of the secretin family form large macromolecular complexes, which assemble in the outer membrane of Gram-negative bacteria. Secretins are major components of type II and III secretion systems and are linked to extrusion of type IV pili (T4P) and to DNA uptake. By electron cryo-tomography of whole Thermus thermophilus cells, we determined the in situ structure of a T4P molecular machine in the open and the closed state. Comparison reveals a major conformational change whereby the N-terminal domains of the central secretin PilQ shift by ∼30 Å, and two periplasmic gates open to make way for pilus extrusion. Furthermore, we determine the structure of the assembled pilus. DOI: http://dx.doi.org/10.7554/eLife.07380.001
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spelling pubmed-44634272015-06-15 Structure of a type IV pilus machinery in the open and closed state Gold, Vicki AM Salzer, Ralf Averhoff, Beate Kühlbrandt, Werner eLife Biophysics and Structural Biology Proteins of the secretin family form large macromolecular complexes, which assemble in the outer membrane of Gram-negative bacteria. Secretins are major components of type II and III secretion systems and are linked to extrusion of type IV pili (T4P) and to DNA uptake. By electron cryo-tomography of whole Thermus thermophilus cells, we determined the in situ structure of a T4P molecular machine in the open and the closed state. Comparison reveals a major conformational change whereby the N-terminal domains of the central secretin PilQ shift by ∼30 Å, and two periplasmic gates open to make way for pilus extrusion. Furthermore, we determine the structure of the assembled pilus. DOI: http://dx.doi.org/10.7554/eLife.07380.001 eLife Sciences Publications, Ltd 2015-05-21 /pmc/articles/PMC4463427/ /pubmed/25997099 http://dx.doi.org/10.7554/eLife.07380 Text en © 2015, Gold et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biophysics and Structural Biology
Gold, Vicki AM
Salzer, Ralf
Averhoff, Beate
Kühlbrandt, Werner
Structure of a type IV pilus machinery in the open and closed state
title Structure of a type IV pilus machinery in the open and closed state
title_full Structure of a type IV pilus machinery in the open and closed state
title_fullStr Structure of a type IV pilus machinery in the open and closed state
title_full_unstemmed Structure of a type IV pilus machinery in the open and closed state
title_short Structure of a type IV pilus machinery in the open and closed state
title_sort structure of a type iv pilus machinery in the open and closed state
topic Biophysics and Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4463427/
https://www.ncbi.nlm.nih.gov/pubmed/25997099
http://dx.doi.org/10.7554/eLife.07380
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AT averhoffbeate structureofatypeivpilusmachineryintheopenandclosedstate
AT kuhlbrandtwerner structureofatypeivpilusmachineryintheopenandclosedstate

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