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3CI0

The Crystal Structure of the GspK-GspI-GspJ complex from enterotoxigenic Escherichia coli Type 2 Secretion System

Summary for 3CI0
Entry DOI10.2210/pdb3ci0/pdb
DescriptorPseudopilin GspI, Pseudopilin GspJ, Pseudopilin GspK, ... (6 entities in total)
Functional Keywordsgeneral secretory pathway, pseudopilus, type 4 pilin biogenesis, methylation, protein transport
Biological sourceEscherichia coli
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Cellular locationCell inner membrane (By similarity): A7ZRI8
Total number of polymer chains3
Total formula weight62640.15
Authors
Korotkov, K.V.,Hol, W.G.J. (deposition date: 2008-03-10, release date: 2008-04-29, Last modification date: 2024-10-16)
Primary citationKorotkov, K.V.,Hol, W.G.
Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system.
Nat.Struct.Mol.Biol., 15:462-468, 2008
Cited by
PubMed 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.
PubMed: 18438417
DOI: 10.1038/nsmb.1426
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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數據於2024-11-13公開中

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