3kd9

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Crystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshiiCrystal structure of pyridine nucleotide disulfide oxidoreductase from Pyrococcus horikoshii

Structural highlights

3kd9 is a 3 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NCPPR_PYRHO Catalyzes the NAD(P)H-dependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides. The likely in vivo substrates are di-, poly-, and persulfide derivatives of coenzyme A, although polysulfide itself is also efficiently reduced (PubMed:23530771). Shows coenzyme A disulfide reductase (CoADR) activity with both NADH and NADPH, with a preference for NADPH (PubMed:15720393). May also play a role in the reduction of elemental sulfur (PubMed:23530771).[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Harris DR, Ward DE, Feasel JM, Lancaster KM, Murphy RD, Mallet TC, Crane EJ 3rd. Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles. FEBS J. 2005 Mar;272(5):1189-200. PMID:15720393 doi:EJB4555
  2. Herwald S, Liu AY, Zhu BE, Sea KW, Lopez KM, Sazinsky MH, Crane Iii EJ. Characterization of the structure and substrate specificity of the pyrococcal CoADR/Psr: Implications for S0-based respiration and a sulfur-dependent antioxidant system in Pyrococcus. Biochemistry. 2013 Mar 26. PMID:23530771 doi:10.1021/bi3014399

3kd9, resolution 2.75Å

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