3jwn | pdb_00003jwn

Complex of FimC, FimF, FimG and FimH

spinqualitylabelsall models 3jwn, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jwn is a 10 chain structure with sequence from Ecoli and Escherichia coli f18+. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Gene: b4316, fimC, JW4279 (ECOLI), b4318, fimF, JW4281 (ECOLI), b4319, fimG, JW4282 (ECOLI), ECP_4655, fimh (Escherichia coli F18+) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. [FIMG_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [FIMF_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. 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 Escherichia coli fimbrial adhesive protein, FimH, mediates shear-dependent binding to mannosylated surfaces via force-enhanced allosteric catch bonds, but the underlying structural mechanism was previously unknown. Here we present the crystal structure of FimH incorporated into the multiprotein fimbrial tip, where the anchoring (pilin) domain of FimH interacts with the mannose-binding (lectin) domain and causes a twist in the beta sandwich fold of the latter. This loosens the mannose-binding pocket on the opposite end of the lectin domain, resulting in an inactive low-affinity state of the adhesin. The autoinhibition effect of the pilin domain is removed by application of tensile force across the bond, which separates the domains and causes the lectin domain to untwist and clamp tightly around the ligand like a finger-trap toy. Thus, beta sandwich domains, which are common in multidomain proteins exposed to tensile force in vivo, can undergo drastic allosteric changes and be subjected to mechanical regulation. Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting.,Le Trong I, Aprikian P, Kidd BA, Forero-Shelton M, Tchesnokova V, Rajagopal P, Rodriguez V, Interlandi G, Klevit R, Vogel V, Stenkamp RE, Sokurenko EV, Thomas WE Cell. 2010 May 14;141(4):645-55. PMID:20478255 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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