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

Tools

Item Type:	Article
Title:	Structure of the dodecameric Yersinia enterocolitica secretin YscC and its trypsin-resistant core
Creators Name:	Kowal, J., Chami, M., Ringler, P., Müller, S.A., Kudryashev, M., Castaño-Díez, D., Amstutz, M., Cornelis, G.R., 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
Source:	Structure
ISSN:	0969-2126
Publisher:	Cell Press
Volume:	21
Number:	12
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

Repository Staff Only: item control page