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Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1300-8. doi: 10.1107/S2053230X15016064. Epub 2015 Sep 23.

Structural analysis of SepL, an enteropathogenic Escherichia coli type III secretion-system gatekeeper protein.

Author information

1
Department of Biochemistry and Molecular Biology, University of British Columbia, Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada.

Abstract

During infection, enteropathogenic Escherichia coli assembles a complex multi-protein type III secretion system that traverses the bacterial membranes and targets the host cell membrane to directly deliver virulence or effector proteins to the host cytoplasm. As this secretion system is composed of more than 20 proteins, many of which form oligomeric associations, its assembly must be tightly regulated. A protein called the gatekeeper, or SepL, ensures that the secretion of the translocon component, which inserts into the host membrane, occurs before the secretion of effectors. The crystal structure of the gatekeeper SepL was determined and compared with the structures of SepL homologues from other bacterial pathogens in order to identify SepL residues that may be critical for its role in type III secretion-system assembly.

KEYWORDS:

bacterial pathogenesis; protein secretion

PMID:
26457522
PMCID:
PMC4601595
DOI:
10.1107/S2053230X15016064
[Indexed for MEDLINE]
Free PMC Article

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