3bfw | pdb_00003bfw

Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)

spinqualitylabelsall models 3bfw, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bfw is a 4 chain structure with sequence from Escherichia coli and Escherichia coli str. K-12 substr. W3110. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: YT3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 Adhesive type 1 pili from uropathogenic Escherichia coli strains are heat and denaturant resistant, filamentous protein complexes. Individual pilus subunits associate through "donor strand complementation," whereby the incomplete immunoglobulin-like fold of each subunit is completed by the N-terminal extension of a neighboring subunit. We show that antiparallel donor strand insertion generally causes nonequilibrium behavior in protein folding and extreme activation energy barriers for dissociation of subunit-subunit complexes. We identify the most kinetically stable, noncovalent protein complex known to date. The complex between the pilus subunit FimG and the donor strand peptide of the subunit FimF shows an extrapolated dissociation half-life of 3 x 10(9) years. The 15 residue peptide forms ideal intermolecular beta sheet H-bonds with FimG over 10 residues, and its hydrophobic side chains strongly interact with the hydrophobic core of FimG. The results show that kinetic stability and nonequilibrium behavior in protein folding confers infinite stability against dissociation in extracellular protein complexes. Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation.,Puorger C, Eidam O, Capitani G, Erilov D, Grutter MG, Glockshuber R Structure. 2008 Apr;16(4):631-42. PMID:18400183 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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