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

Kowal, Julia and Chami, Mohamed and Ringler, Philippe and Müller, Shirley A. and Kudryashev, Mikhail and Castaño-Díez, Daniel and Amstutz, Marlise and Cornelis, Guy R. and Stahlberg, Henning and Engel, Andreas. (2013) Structure of the Dodecameric Yersinia enterocolitica Secretin YscC and Its Trypsin-Resistant Core. Structure, 21 (12). pp. 2152-2161.

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Official URL: http://edoc.unibas.ch/dok/A6205311

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Stahlberg)
05 Faculty of Science > Departement Biozentrum > Services Biozentrum > BioEM Lab (Chami)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology and Biophysics (Engel)
UniBasel Contributors:Stahlberg, Henning and Ringler, Philippe and Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cell Press
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:16 Mar 2023 11:39
Deposited On:31 Jan 2014 09:49

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