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

Résultats de recherche: Contribution à un journal/une revueArticleRevue par des pairs

Résumé

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.
langue originaleAnglais
Pages (de - à)2152-61
Nombre de pages10
journalStructure (London, England : 1993)
Volume21
Numéro de publication12
Les DOIs
Etat de la publicationPublié - 3 déc. 2013

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