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Structure of the cholera toxin secretion channel in its closed state

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 like cholera toxin and heat-labile enterotoxin from Vibrio cholerae and enterotoxigenic Esch...

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Autores principales: Reichow, Steve L., Korotkov, Konstantin V., Hol, Wim G. J., Gonen, Tamir
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2950906/
https://www.ncbi.nlm.nih.gov/pubmed/20852644
http://dx.doi.org/10.1038/nsmb.1910
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author Reichow, Steve L.
Korotkov, Konstantin V.
Hol, Wim G. J.
Gonen, Tamir
author_facet Reichow, Steve L.
Korotkov, Konstantin V.
Hol, Wim G. J.
Gonen, Tamir
author_sort Reichow, Steve L.
collection PubMed
description 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 like cholera toxin and heat-labile enterotoxin from Vibrio cholerae and enterotoxigenic Escherichia coli, respectively. The major outer membrane T2SS protein is the “secretin” GspD. Electron cryomicroscopy 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 appears to contain a closed periplasmic gate. The GspD periplasmic domain forms a vestibule with a conserved constriction, and 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, we provide a structural basis for a possible secretion mechanism of the T2SS.
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spelling pubmed-29509062011-04-01 Structure of the cholera toxin secretion channel in its closed state Reichow, Steve L. Korotkov, Konstantin V. Hol, Wim G. J. Gonen, Tamir Nat Struct Mol Biol Article 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 like cholera toxin and heat-labile enterotoxin from Vibrio cholerae and enterotoxigenic Escherichia coli, respectively. The major outer membrane T2SS protein is the “secretin” GspD. Electron cryomicroscopy 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 appears to contain a closed periplasmic gate. The GspD periplasmic domain forms a vestibule with a conserved constriction, and 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, we provide a structural basis for a possible secretion mechanism of the T2SS. 2010-09-19 2010-10 /pmc/articles/PMC2950906/ /pubmed/20852644 http://dx.doi.org/10.1038/nsmb.1910 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Reichow, Steve L.
Korotkov, Konstantin V.
Hol, Wim G. J.
Gonen, Tamir
Structure of the cholera toxin secretion channel in its closed state
title Structure of the cholera toxin secretion channel in its closed state
title_full Structure of the cholera toxin secretion channel in its closed state
title_fullStr Structure of the cholera toxin secretion channel in its closed state
title_full_unstemmed Structure of the cholera toxin secretion channel in its closed state
title_short Structure of the cholera toxin secretion channel in its closed state
title_sort structure of the cholera toxin secretion channel in its closed state
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2950906/
https://www.ncbi.nlm.nih.gov/pubmed/20852644
http://dx.doi.org/10.1038/nsmb.1910
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