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Nat Struct Mol Biol. 2010 Oct;17(10):1226-32. doi: 10.1038/nsmb.1910. Epub 2010 Sep 19.

Structure of the cholera toxin secretion channel in its closed state.

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1
Department of Biochemistry, University of Washington, Seattle, Washington, USA.

Abstract

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.

PMID:
20852644
PMCID:
PMC2950906
DOI:
10.1038/nsmb.1910
[Indexed for MEDLINE]
Free PMC Article
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