Structure of the Dodecameric Yersinia enterocolitica Secretin YscC and Its Trypsin-Resistant Core

Julia Kowal, Mohamed Chami, Philippe Ringler, Shirley A Müller, Mikhail Kudryashev, Daniel Castaño-Díez, Marlise Amstutz, Guy R Cornelis, Henning Stahlberg, Andreas Engel

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)2152-61
Number of pages10
JournalStructure (London, England : 1993)
Volume21
Issue number12
DOIs
Publication statusPublished - 3 Dec 2013

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