Kowal, JuliaChami, MohamedRingler, PhilippeMueller, Shirley A.Kudryashev, MikhailCastano-Diez, DanielAmstutz, MarliseCornelis, Guy R.Stahlberg, HenningEngel, Andreas2020-02-132020-02-132020-02-132013-12-0110.1016/j.str.2013.09.012https://infoscience.epfl.ch/handle/20.500.14299/165360The type Ill 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 A 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.text::journal::journal article::research article