4nv2

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C50A mutant of Synechococcus VKOR, C2221 crystal form

Structural highlights

4nv2 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 3.61Å
Ligands: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.[1] [2]

Publication Abstract from PubMed

The intramembrane vitamin K epoxide reductase (VKOR) supports blood coagulation in humans and is the target of the anticoagulant warfarin. VKOR and its homologues generate disulphide bonds in organisms ranging from bacteria to humans. Here, to better understand the mechanism of VKOR catalysis, we report two crystal structures of a bacterial VKOR captured in different reaction states. These structures reveal a short helix at the hydrophobic active site of VKOR that alters between wound and unwound conformations. Motions of this 'horizontal helix' promote electron transfer by regulating the positions of two cysteines in an adjacent loop. Winding of the helix separates these 'loop cysteines' to prevent backward electron flow. Despite these motions, hydrophobicity at the active site is maintained to facilitate VKOR catalysis. Biochemical experiments suggest that several warfarin-resistant mutations act by changing the conformation of the horizontal helix. Taken together, these studies provide a comprehensive understanding of VKOR function.

Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer.,Liu S, Cheng W, Fowle Grider R, Shen G, Li W Nat Commun. 2014 Jan 29;5:3110. doi: 10.1038/ncomms4110. PMID:24477003[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
6 reviews cite this structure
Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
Fass et al. (2018)
5 more
18 other articles
No citations found

References

  1. ↑ Li W, Schulman S, Dutton RJ, Boyd D, Beckwith J, Rapoport TA. Structure of a bacterial homologue of vitamin K epoxide reductase. Nature. 2010 Jan 28;463(7280):507-12. PMID:20110994 doi:10.1038/nature08720
  2. ↑ Liu S, Cheng W, Fowle Grider R, Shen G, Li W. Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer. Nat Commun. 2014 Jan 29;5:3110. doi: 10.1038/ncomms4110. PMID:24477003 doi:http://dx.doi.org/10.1038/ncomms4110
  3. ↑ Liu S, Cheng W, Fowle Grider R, Shen G, Li W. Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer. Nat Commun. 2014 Jan 29;5:3110. doi: 10.1038/ncomms4110. PMID:24477003 doi:http://dx.doi.org/10.1038/ncomms4110

Contents


PDB ID 4nv2

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