Crystal structure analysis of formate oxidaseCrystal structure analysis of formate oxidase

Structural highlights

3q9t is a 3 chain structure with sequence from Aspergillus oryzae RIB40. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.24Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q2UD26_ASPOR

Publication Abstract from PubMed

Formate oxidase of Aspergillus oryzae RIB40 contains an 8-replaced FAD with molecular mass of 799 as cofactor. The (1)H-NMR spectrum of the cofactor fraction obtained from the enzyme indicated that the 8-replaced FAD in the fraction was 8-formyl-FAD, present in open form and hemiacetal form. The oxidation-reduction potentials of the open and hemiacetal forms were estimated by cyclic voltammetry to be -47 and -177 mV vs. Normal Hydrogen Electrode respectively. The structure of the enzyme was constructed using diffraction data to 2.24 A resolution collected from a crystal of the enzyme. His(511) and Arg(554) were situated close to the pyrimidine part of the isoalloxazine ring of 8-formyl-FAD in open form. The enzyme had 8-formyl-FAD, the oxidation potential of which was approximately 160 mV more positive than that of FAD, and the His-Arg pair at the catalytic site, unlike the other enzymes belonging to the glucose-methanol-choline oxidoreductase family.

Formate Oxidase, an Enzyme of the Glucose-Methanol-Choline Oxidoreductase Family, Has a His-Arg Pair and 8-Formyl-FAD at the Catalytic Site.,Doubayashi D, Ootake T, Maeda Y, Oki M, Tokunaga Y, Sakurai A, Nagaosa Y, Mikami B, Uchida H Biosci Biotechnol Biochem. 2011 Sep 7. PMID:21897046[1]

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

References

  1. Doubayashi D, Ootake T, Maeda Y, Oki M, Tokunaga Y, Sakurai A, Nagaosa Y, Mikami B, Uchida H. Formate Oxidase, an Enzyme of the Glucose-Methanol-Choline Oxidoreductase Family, Has a His-Arg Pair and 8-Formyl-FAD at the Catalytic Site. Biosci Biotechnol Biochem. 2011 Sep 7. PMID:21897046

3q9t, resolution 2.24Å

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