Structural highlights
4dwh 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.
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| Ligands: | , , , |
| Related: | 3sqb |
| Gene: | b4316, fimC, JW4279 ("Bacillus coli" Migula 1895), b4314, fimA, JW4277, pilA ("Bacillus coli" Migula 1895) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. [FIMA1_ECOLI] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
Publication Abstract from PubMed
Type 1 pili from uropathogenic Escherichia coli are filamentous, noncovalent protein complexes mediating bacterial adhesion to the host tissue. All structural pilus subunits are homologous proteins sharing an invariant disulfide bridge. Here we show that disulfide bond formation in the unfolded subunits, catalyzed by the periplasmic oxidoreductase DsbA, is required for subunit recognition by the assembly chaperone FimC and for FimC-catalyzed subunit folding. FimC thus guarantees quantitative disulfide bond formation in each of the up to 3,000 subunits of the pilus. The X-ray structure of the complex between FimC and the main pilus subunit FimA and the kinetics of FimC-catalyzed FimA folding indicate that FimC accelerates folding of pilus subunits by lowering their topological complexity. The kinetic data, together with the measured in vivo concentrations of DsbA and FimC, predict an in vivo half-life of 2 s for oxidative folding of FimA in the periplasm.
Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.,Crespo MD, Puorger C, Scharer MA, Eidam O, Grutter MG, Capitani G, Glockshuber R Nat Chem Biol. 2012 Jul 1. doi: 10.1038/nchembio.1019. PMID:22772153[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Crespo MD, Puorger C, Scharer MA, Eidam O, Grutter MG, Capitani G, Glockshuber R. Quality control of disulfide bond formation in pilus subunits by the chaperone FimC. Nat Chem Biol. 2012 Jul 1. doi: 10.1038/nchembio.1019. PMID:22772153 doi:10.1038/nchembio.1019
