3oss

The crystal structure of enterotoxigenic Escherichia coli GspC-GspD complex from the type II secretion system

spinqualitylabelsall models 3oss, resolution 2.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3oss is a 2 chain structure with sequence from Escherichia coli ETEC H10407. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.63Å Ligands: CA, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GSPD2_ECOH1 Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable). Publication Abstract from PubMed Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-beta topology. N-terminal beta-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed. Structural and functional studies on the interaction of GspC and GspD in the type II secretion system.,Korotkov KV, Johnson TL, Jobling MG, Pruneda J, Pardon E, Heroux A, Turley S, Steyaert J, Holmes RK, Sandkvist M, Hol WG PLoS Pathog. 2011 Sep;7(9):e1002228. Epub 2011 Sep 8. PMID:21931548 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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