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The Crystal Structure of the GspK-GspI-GspJ complex from enterotoxigenic Escherichia coli Type 2 Secretion SystemThe Crystal Structure of the GspK-GspI-GspJ complex from enterotoxigenic Escherichia coli Type 2 Secretion System
Structural highlights
FunctionGSPI_ECOLX Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates.[UniProtKB:Q00516] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGram-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. Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system.,Korotkov KV, Hol WG Nat Struct Mol Biol. 2008 May;15(5):462-8. Epub 2008 Apr 27. PMID:18438417[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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