1JZD
DsbC-DsbDalpha complex
Summary for 1JZD
| Entry DOI | 10.2210/pdb1jzd/pdb |
| Related | 1eej 1jzo |
| Descriptor | thiol:disulfide interchange protein dsbc, thiol:disulfide interchange protein dsbd (3 entities in total) |
| Functional Keywords | thiol disulfide oxidoreductase, reaction intermediate, protein-protein complex, oxidoreductase |
| Biological source | Escherichia coli More |
| Cellular location | Periplasm: P21892 Cell inner membrane; Multi-pass membrane protein: P36655 |
| Total number of polymer chains | 3 |
| Total formula weight | 62377.09 |
| Authors | Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P. (deposition date: 2001-09-15, release date: 2003-03-08, Last modification date: 2023-08-16) |
| Primary citation | Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P. The Disulfide Bond Isomerase DsbC is Activated by an Immunoglobulin-fold Thiol Oxidoreductase: Crystal structure of the DsbC-DsbDalpha complex. Embo J., 21:4774-4784, 2002 Cited by PubMed Abstract: The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm. PubMed: 12234918DOI: 10.1093/emboj/cdf489 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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