3gew | pdb_00003gew

FaeE-FaeG chaperone-major pilin complex of F4 ad fimbriae

spinqualitylabelsall models 3gew, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gew is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4 Related: 3f65, 3f6i, 3f6l, 2j6g, 2j6r, 3gea, 3gfu, 3ggh, 3hlr Gene: faeE ("Bacillus coli" Migula 1895), faeG ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [FAEE_ECOLX] Mediates assembly of pili by forming soluble multimeric complexes with pili subunits as an intermediate step in the assembly process. This protein is involved in K88 pili assembly. Protects pilin protein from proteolytic degradation by DegP and from premature polymerization. [FAEG3_ECOLX] K88 major fimbrial subunit. Fimbriae (also called 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. They 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 Enterotoxigenic Escherichia coli expressing F4 fimbriae are the major cause of porcine colibacillosis and are responsible for significant death and morbidity in neonatal and postweaned piglets. Via the chaperone-usher pathway, F4 fimbriae are assembled into thin, flexible polymers mainly composed of the single-domain adhesin FaeG. The F4 fimbrial system has been labeled eccentric because the F4 pilins show some features distinct from the features of pilins of other chaperone-usher-assembled structures. In particular, FaeG is much larger than other pilins (27 versus approximately 17 kDa), grafting an additional carbohydrate binding domain on the common immunoglobulin-like core. Structural data of FaeG during different stages of the F4 fimbrial biogenesis process, combined with differential scanning calorimetry measurements, confirm the general principles of the donor strand complementation/exchange mechanisms taking place during pilus biogenesis via the chaperone-usher pathway. Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG.,Van Molle I, Moonens K, Garcia-Pino A, Buts L, De Kerpel M, Wyns L, Bouckaert J, De Greve H J Mol Biol. 2009 Dec 18;394(5):957-67. Epub 2009 Sep 30. PMID:19799915 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pilin

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