2wmp | pdb_00002wmp

Structure of the E. coli chaperone PapD in complex with the pilin domain of the PapGII adhesin

spinqualitylabelsall models 2wmp, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wmp is a 2 chain structure with sequence from Escherichia coli and Escherichia coli uti89. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1qpp, 1qpx, 1pdk, 3dpa, 1n0l, 3me0 Resources: FirstGlance, OCA, RCSB, PDBsum 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 hairlike polymeric structures that mediate binding of uropathogenic Escherichia coli to the surface of the kidney via the PapG adhesin at their tips. PapG is composed of two domains: a lectin domain at the tip of the pilus followed by a pilin domain that comprises the initial polymerizing subunit of the 1000-plus-subunit heteropolymeric pilus fiber. Prior to assembly, periplasmic pilin domains bind to a chaperone, PapD. PapD mediates donor strand complementation, in which a beta strand of PapD temporarily completes the pilin domain's fold, preventing premature, non-productive interactions with other pilin subunits and facilitating subunit folding. Chaperone/subunit complexes are delivered to the outer membrane usher where donor strand exchange (DSE) replaces PapD's donated beta strand with an amino terminal extension on the next incoming pilin subunit. This occurs via a zip-in-zip-out mechanism that initiates at a relatively accessible hydrophobic space termed the P5 pocket on the terminally incorporated pilus subunit. Here, we solve the structure of PapD in complex with the pilin domain of isoform II of PapG (PapGIIp). Our data revealed that PapGIIp adopts an immunoglobulin fold with a missing seventh strand, complemented in parallel by the G1 PapD strand, typical of pilin subunits. Comparisons with other chaperone/pilin complexes indicated that the interactive surfaces are highly conserved. Interestingly, the PapGIIp P5 pocket was in an open conformation, which, as molecular dynamics simulations revealed, switches between an "open" and "closed" conformation due to the flexibility of the surrounding loops. Our study reveals the structural details of the DSE mechanism. Structure of the PapD-PapGII pilin complex reveals an open and flexible P5 pocket.,Ford B, Verger D, Dodson K, Volkan E, Kostakioti M, Elam J, Pinkner J, Waksman G, Hultgren S J Bacteriol. 2012 Sep 21. PMID:23002225 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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