3SQB
Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone
Summary for 3SQB
| Entry DOI | 10.2210/pdb3sqb/pdb |
| Related | 2jty 4DWH |
| Descriptor | Chaperone protein fimC, Type-1 fimbrial protein, A chain, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| Functional Keywords | immunoglobin-like fold, involved in type 1 pilus assembly, structural protein-chaperone complex, structural protein/chaperone |
| Biological source | Escherichia coli More |
| Cellular location | Periplasm: P31697 Fimbrium: P04128 |
| Total number of polymer chains | 8 |
| Total formula weight | 156529.18 |
| Authors | Scharer, M.A.,Eidam, O.,Grutter, M.G.,Glockshuber, R.,Capitani, G. (deposition date: 2011-07-05, release date: 2012-05-30, Last modification date: 2024-10-30) |
| Primary citation | Crespo, M.D.,Puorger, C.,Scharer, M.A.,Eidam, O.,Grutter, M.G.,Capitani, G.,Glockshuber, R. Quality control of disulfide bond formation in pilus subunits by the chaperone FimC. Nat.Chem.Biol., 8:707-713, 2012 Cited by PubMed Abstract: 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. PubMed: 22772153DOI: 10.1038/nchembio.1019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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