2kep

Solution structure of XcpT, the main component of the type 2 secretion system of Pseudomonas aeruginosa

spinqualitylabelsall models 2kep Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kep is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GSPG_PSEAE Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for the translocation of a variety of enzymes across 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 The bacterial type II protein secretion (T2S) and type IV piliation (T4P) systems share several common features. In particular, it is well established that the T2S system requires the function of a pilus-like structure, called pseudopilus, which is built upon assembly of pilin-like subunits, called pseudopilins. Pilins and pseudopilins have a hydrophobic N-terminal region, which precedes an extended hydrophilic C-terminal region. In the case of pilins, it was shown that oligomerisation and formation of helical fibers, takes place through interaction between the hydrophobic domains. XcpT, is the most abundant protein of the Pseudomonas aeruginosa T2S, and was proposed to be the main component in the pseudopilus. In this study we present the high-resolution NMR structure of the hydrophilic domain of XcpT (XcpTp). XcpTp is lacking the C-terminal disulfide bridged "D" domain found in type IV pilins and likely involved in receptor binding. This is in agreement with the idea that the XcpT-containing pseudopilus is required for protein secretion and not for bacterial attachment. Interestingly, by solving the 3D structure of XcpTp we revealed that the previously called alphabeta-loop pilin region is in fact highly conserved among major type II pseudopilins and constitutes a specific consensus motif for identifying major pseudopilins, which belong to this family. Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system.,Alphonse S, Durand E, Douzi B, Waegele B, Darbon H, Filloux A, Voulhoux R, Bernard C J Struct Biol. 2010 Jan;169(1):75-80. Epub 2009 Sep 9. PMID:19747550 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pseudopilin

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