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 α-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.
Original language | English |
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Pages (from-to) | 462-468 |
Number of pages | 7 |
Journal | Nature Structural and Molecular Biology |
Volume | 15 |
Issue number | 5 |
DOIs | |
State | Published - May 2008 |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology