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

Structure. 2013 Dec 3;21(12):2152-61. doi: 10.1016/j.str.2013.09.012. Epub 2013 Oct 24.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Lipid Bilayers / chemistry
  • Models, Molecular
  • Osmotic Pressure
  • Protein Conformation
  • Protein Multimerization
  • Secretin / chemistry*
  • Secretin / genetics
  • Secretin / metabolism
  • Trypsin / metabolism*
  • Yersinia enterocolitica / metabolism*

Substances

  • Bacterial Proteins
  • Lipid Bilayers
  • Secretin
  • Trypsin