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 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.
Author:Vicki A. M. Gold, Ralf Salzer, Beate AverhoffORCiD, Werner Kühlbrandt
Pubmed Id:
Parent Title (English):eLife
Publisher:eLife Sciences Publications
Place of publication:Cambridge
Contributor(s):Stephen C. Harrison
Document Type:Article
Date of Publication (online):2017/05/22
Year of first Publication:2015
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2017/05/22
Tag:DNA transporter; Thermus thermophilus; bacterial secretion; biophysics; electron cryo-tomography; structural biology; subtomogram averaging; type IV pilus
Page Number:12
First Page:1
Last Page:12
Copyright Gold et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
Institutes:Biowissenschaften / Biowissenschaften
Angeschlossene und kooperierende Institutionen / MPI für Biophysik
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Licence (German):License LogoCreative Commons - Namensnennung 4.0