2uy6 | pdb_00002uy6

Crystal structure of the P pilus rod subunit PapA

spinqualitylabelsall models 2uy6, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2uy6 is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Ecout. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1n0l, 1pdk, 1qpp, 1qpx, 2j2z, 2j7l, 3dpa Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PAPA_ECOLX] Polymerizes to form the thick (6.8 nm in diameter) rod of the pilus (also called fimbria). The rod is a right-handed helical cylinder with 3.28 PapA subunits per turn. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs. 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 P pili are important adhesive fibres involved in kidney infection by uropathogenic Escherichia coli strains. P pili are assembled by the conserved chaperone-usher pathway, which involves the PapD chaperone and the PapC usher. During pilus assembly, subunits are incorporated into the growing fiber via the donor-strand exchange (DSE) mechanism, whereby the chaperone's G1 beta-strand that complements the incomplete immunoglobulin-fold of each subunit is displaced by the N-terminal extension (Nte) of an incoming subunit. P pili comprise a helical rod, a tip fibrillum, and an adhesin at the distal end. PapA is the rod subunit and is assembled into a superhelical right-handed structure. Here, we have solved the structure of a ternary complex of PapD bound to PapA through donor-strand complementation, itself bound to another PapA subunit through DSE. This structure provides insight into the structural basis of the DSE reaction involving this important pilus subunit. Using gel filtration chromatography and electron microscopy on a number of PapA Nte mutants, we establish that PapA differs in its mode of assembly compared with other Pap subunits, involving a much larger Nte that encompasses not only the DSE region of the Nte but also the region N-terminal to it. Crystal structure of the P pilus rod subunit PapA.,Verger D, Bullitt E, Hultgren SJ, Waksman G PLoS Pathog. 2007 May 18;3(5):e73. PMID:17511517 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pilin 3D structures

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