TY - JOUR
T1 - Structure of the Dodecameric Yersinia enterocolitica Secretin YscC and Its Trypsin-Resistant Core
AU - Kowal, Julia
AU - Chami, Mohamed
AU - Ringler, Philippe
AU - Müller, Shirley A
AU - Kudryashev, Mikhail
AU - Castaño-Díez, Daniel
AU - Amstutz, Marlise
AU - Cornelis, Guy R
AU - Stahlberg, Henning
AU - Engel, Andreas
N1 - Copyright © 2013 Elsevier Ltd. All rights reserved.
PY - 2013/12/3
Y1 - 2013/12/3
N2 - 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.
AB - 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.
U2 - 10.1016/j.str.2013.09.012
DO - 10.1016/j.str.2013.09.012
M3 - Article
C2 - 24207124
SN - 1878-4186
VL - 21
SP - 2152
EP - 2161
JO - Structure (London, England : 1993)
JF - Structure (London, England : 1993)
IS - 12
ER -