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TitleStructure of the cholera toxin secretion channel in its closed state.
Journal, issue, pagesNat Struct Mol Biol, Vol. 17, Issue 10, Page 1226-1232, Year 2010
Publish dateSep 19, 2010
AuthorsSteve L Reichow / Konstantin V Korotkov / Wim G J Hol / Tamir Gonen /
PubMed AbstractThe type II secretion system (T2SS) is a macromolecular complex spanning the inner and outer membranes of Gram-negative bacteria. Remarkably, the T2SS secretes folded proteins, including multimeric ...The type II secretion system (T2SS) is a macromolecular complex spanning the inner and outer membranes of Gram-negative bacteria. Remarkably, the T2SS secretes folded proteins, including multimeric assemblies such as cholera toxin and heat-labile enterotoxin from Vibrio cholerae and enterotoxigenic Escherichia coli, respectively. The major outer membrane T2SS protein is the 'secretin' GspD. Cryo-EM reconstruction of the V. cholerae secretin at 19-Å resolution reveals a dodecameric structure reminiscent of a barrel, with a large channel at its center that contains a closed periplasmic gate. The GspD periplasmic domain forms a vestibule with a conserved constriction, and it binds to a pentameric exoprotein and to the trimeric tip of the T2SS pseudopilus. By combining our results with structures of the cholera toxin and T2SS pseudopilus tip, we provide a structural basis for a possible secretion mechanism of the T2SS.
External linksNat Struct Mol Biol / PubMed:20852644 / PubMed Central
MethodsEM (single particle)
Resolution19.0 Å
Structure data

EMDB-1763:
3D reconstruction of the type ii secretin GspD from Vibrio cholera
Method: EM (single particle) / Resolution: 19.0 Å

Source
  • Vibrio cholerae (bacteria)

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