3KP8
The thioredoxin-like domain of a VKOR homolog from Synechococcus sp.
Summary for 3KP8
| Entry DOI | 10.2210/pdb3kp8/pdb |
| Related | 3KP9 |
| Descriptor | VKORC1/thioredoxin domain protein (2 entities in total) |
| Functional Keywords | blood coagulation, disulfide formation, redox partner, oxidoreductase |
| Biological source | Synechococcus sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 11570.85 |
| Authors | Li, W.,Schulman, S.,Dutton, R.J.,Boyd, D.,Beckwith, J.,Rapoport, T.A. (deposition date: 2009-11-15, release date: 2010-03-02, Last modification date: 2024-11-20) |
| Primary citation | Li, W.,Schulman, S.,Dutton, R.J.,Boyd, D.,Beckwith, J.,Rapoport, T.A. Structure of a bacterial homologue of vitamin K epoxide reductase. Nature, 463:507-512, 2010 Cited by PubMed Abstract: Vitamin K epoxide reductase (VKOR) generates vitamin K hydroquinone to sustain gamma-carboxylation of many blood coagulation factors. Here, we report the 3.6 A crystal structure of a bacterial homologue of VKOR from Synechococcus sp. The structure shows VKOR in complex with its naturally fused redox partner, a thioredoxin-like domain, and corresponds to an arrested state of electron transfer. The catalytic core of VKOR is a four transmembrane helix bundle that surrounds a quinone, connected through an additional transmembrane segment with the periplasmic thioredoxin-like domain. We propose a pathway for how VKOR uses electrons from cysteines of newly synthesized proteins to reduce a quinone, a mechanism confirmed by in vitro reconstitution of vitamin K-dependent disulphide bridge formation. Our results have implications for the mechanism of the mammalian VKOR and explain how mutations can cause resistance to the VKOR inhibitor warfarin, the most commonly used oral anticoagulant. PubMed: 20110994DOI: 10.1038/nature08720 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.66 Å) |
Structure validation
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