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Structure of the dodecameric Yersinia enterocolitica secretin YscC and its trypsin-resistant core

Item Type:Article
Title:Structure of the dodecameric Yersinia enterocolitica secretin YscC and its trypsin-resistant core
Creators Name:Kowal, J. and Chami, M. and Ringler, P. and Müller, S.A. and Kudryashev, M. and Castaño-Díez, D. and Amstutz, M. and Cornelis, G.R. and Stahlberg, H. and Engel, A.
Abstract:The type III secretion system machinery, also known as the injectisome, delivers bacterial effector proteins into eukaryotic cells during infection. The outer membrane YscC secretin is a major part of Yersinia enterocolitica's injectisome and is among the first components to assemble, solely assisted by its pilotin, YscW. We have determined the three-dimensional structures of the native complex and its protease-resistant core to 12 Å resolution by cryo-electron microscopy (cryo-EM) and show that YscC forms a dodecameric complex. Cryo-EM of YscC reconstituted into proteoliposomes defines the secretin's membrane-spanning region. Native YscC consists of an outer membrane ring connected via a thin cylindrical wall to a conical, periplasmic region that exposes N-terminal petals connected by flexible linkers. These petals harbor the binding site of YscD, a component of the inner membrane ring. A change in their orientation adapts the length of the YscC secretin and facilitates its interaction with YscD.
Keywords:Bacterial Proteins, Lipid Bilayers, Molecular Models, Osmotic Pressure, Protein Conformation, Protein Multimerization, Secretin, Trypsin, Yersinia enterocolitica
Publisher:Cell Press
Page Range:2152-2161
Date:3 December 2013
Official Publication:https://doi.org/10.1016/j.str.2013.09.012
PubMed:View item in PubMed

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