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| Item Type: | Article |
|---|---|
| Title: | Structure of the dodecameric Yersinia enterocolitica secretin YscC and its trypsin-resistant core |
| Creators Name: | Kowal, J., Chami, M., Ringler, P., Müller, S.A., Kudryashev, M., Castaño-Díez, D., Amstutz, M., Cornelis, G.R., Stahlberg, H. and Engel, A. |
| 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. |
| Keywords: | Bacterial Proteins, Lipid Bilayers, Molecular Models, Osmotic Pressure, Protein Conformation, Protein Multimerization, Secretin, Trypsin, Yersinia enterocolitica |
| Source: | Structure |
| ISSN: | 0969-2126 |
| Publisher: | Cell Press |
| Volume: | 21 |
| Number: | 12 |
| Page Range: | 2152-2161 |
| Date: | 3 December 2013 |
| Official Publication: | https://doi.org/10.1016/j.str.2013.09.012 |
| PubMed: | View item in PubMed |
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