2qv8

Structure of the minor pseudopilin EpsH from the Type 2 Secretion System of Vibrio choleraeStructure of the minor pseudopilin EpsH from the Type 2 Secretion System of Vibrio cholerae

Structural highlights 2qv8 is a 2 chain structure with sequence from "bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: Gene: epsH ("Bacillo virgola del Koch" Trevisan 1884) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GSPH_VIBCH] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for secretion of cholera toxin through the outer membrane. 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 PubMed Many Gram-negative bacteria use the multi-protein type II secretion system (T2SS) to selectively translocate virulence factors from the periplasmic space into the extracellular environment. In Vibrio cholerae the T2SS is called the extracellular protein secretion (Eps) system,which translocates cholera toxin and several enzymes in their folded state across the outer membrane. Five proteins of the T2SS, the pseudopilins, are thought to assemble into a pseudopilus, which may control the outer membrane pore EpsD, and participate in the active export of proteins in a "piston-like" manner. We report here the 2.0 A resolution crystal structure of an N-terminally truncated variant of EpsH, a minor pseudopilin from Vibrio cholerae. While EpsH maintains an N-terminal alpha-helix and C-terminal beta-sheet consistent with the type 4a pilin fold, structural comparisons reveal major differences between the minor pseudopilin EpsH and the major pseudopilin GspG from Klebsiella oxytoca: EpsH contains a large beta-sheet in the variable domain, where GspG contains an alpha-helix. Most importantly, EpsH contains at its surface a hydrophobic crevice between its variable and conserved beta-sheets, wherein a majority of the conserved residues within the EpsH family are clustered. In a tentative model of a T2SS pseudopilus with EpsH at its tip, the conserved crevice faces away from the helix axis. This conserved surface region may be critical for interacting with other proteins from the T2SS machinery. Structure of the minor pseudopilin EpsH from the Type 2 secretion system of Vibrio cholerae.,Yanez ME, Korotkov KV, Abendroth J, Hol WG J Mol Biol. 2008 Mar 14;377(1):91-103. Epub 2007 Aug 23. PMID:18241884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pseudopilin

spinqualitylabelsall models 2qv8, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image