3nje

Structure of the Minor Pseudopilin XcpW from the Pseudomonas aeruginosa Type II Secretion System

spinqualitylabelsall models 3nje, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nje is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GSPJ_PSEAE Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for the translocation of a variety of enzymes across the outer membrane. Publication Abstract from PubMed Pseudomonas aeruginosa utilizes the type II secretion machinery to transport virulence factors through the outer membrane into the extracellular space. Five proteins in the type II secretion system share sequence homology with pilin subunits of type IV pili and are called the pseudopilins. The major pseudopilin XcpT(G) assembles into an intraperiplasmic pilus and is thought to act in a piston-like manner to push substrates through an outer membrane secretin. The other four minor pseudopilins, XcpU(H), XcpV(I), XcpW(J) and XcpX(K), play less well defined roles in pseudopilus formation. It was recently discovered that these four minor pseudopilins form a quaternary complex that is presumed to initiate the formation of the pseudopilus and to localize to its tip. Here, the structure of XcpW(J) was refined to 1.85 A resolution. The structure revealed the type IVa pilin fold with an embellished variable antiparallel beta-sheet as also found in the XcpW(J) homologue enterotoxigenic Escherichia coli GspJ(W) and the XcpU(H) homologue Vibrio cholerae EpsU(H). It is proposed that the exposed surface of this sheet may cradle the long N-terminal alpha1 helix of another pseudopilin. The final 31 amino acids of the XcpW(J) structure are instrinsically disordered. Deletion of this unstructured region of XcpW(J) did not prevent type II secretion in vivo. Structure of the minor pseudopilin XcpW from the Pseudomonas aeruginosa type II secretion system.,Franz LP, Douzi B, Durand E, Dyer DH, Voulhoux R, Forest KT Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):124-30. Epub 2011, Jan 15. PMID:21245534 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pseudopilin

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