Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system - PubMed (original) (raw)
doi: 10.1038/nsmb.1426. Epub 2008 Apr 27.
Affiliations
- PMID: 18438417
- DOI: 10.1038/nsmb.1426
Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system
Konstantin V Korotkov et al. Nat Struct Mol Biol. 2008 May.
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.
Comment in
- The type II secretion arrowhead: the structure of GspI-GspJ-GspK.
Forest KT. Forest KT. Nat Struct Mol Biol. 2008 May;15(5):428-30. doi: 10.1038/nsmb0508-428. Nat Struct Mol Biol. 2008. PMID: 18461043 No abstract available.
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