3kp9

Structure of a bacterial homolog of vitamin K epoxide reductase

spinqualitylabelsall models 3kp9, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kp9 is a 1 chain structure with sequence from Synechococcus sp. JA-2-3B'a(2-13). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.6Å Ligands: HG, U10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VKOR_SYNJB Thiol-disulfide oxidoreductase that catalyzes vitamin K-dependent disulfide bond formation in periplasmic target proteins. 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 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. Structure of a bacterial homologue of vitamin K epoxide reductase.,Li W, Schulman S, Dutton RJ, Boyd D, Beckwith J, Rapoport TA Nature. 2010 Jan 28;463(7280):507-12. PMID:20110994 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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