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Nat Struct Mol Biol. 2008 May;15(5):462-8. doi: 10.1038/nsmb.1426. Epub 2008 Apr 27.

Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system.

Author information

1
Department of Biochemistry, Biomolecular Structure Center, University of Washington, Box 357742, Seattle, Washington 98195, USA.

Abstract

Gram-negative bacteria translocate various proteins including virulence factors across their outer membrane via type 2 secretion systems (T2SSs). T2SSs are thought to contain a pseudopilus, a subcomplex formed by one major and several minor pseudopilins. We report the crystal structure of the complex formed by three minor pseudopilins from enterotoxigenic Escherichia coli. The GspK-GspI-GspJ complex has quasihelical characteristics and an architecture consistent with a localization at the pseudopilus tip. The alpha-domain of GspK has a previously unobserved fold with an unexpected dinuclear metal binding site. The area surrounding its disulfide bridge is conserved and might interact with other T2SS components or with secreted proteins.

PMID:
18438417
DOI:
10.1038/nsmb.1426
[Indexed for MEDLINE]

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