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TitleUnderstanding the Molecular Mechanism Underlying the High Catalytic Activity ofp-Hydroxybenzoate Hydroxylase Mutants for Producing Gallic Acid.
Journal, issue, pagesBiochemistry, Vol. 58, Page 4543-4558, Year 2019
Publish dateApr 12, 2019 (structure data deposition date)
AuthorsMoriwaki, Y. / Yato, M. / Terada, T. / Saito, S. / Nukui, N. / Iwasaki, T. / Nishi, T. / Kawaguchi, Y. / Okamoto, K. / Arakawa, T. ...Moriwaki, Y. / Yato, M. / Terada, T. / Saito, S. / Nukui, N. / Iwasaki, T. / Nishi, T. / Kawaguchi, Y. / Okamoto, K. / Arakawa, T. / Yamada, C. / Fushinobu, S. / Shimizu, K.
External linksBiochemistry / PubMed:31639299
MethodsX-ray diffraction
Resolution1.6 Å
Structure data

PDB-6ju1:
p-Hydroxybenzoate hydroxylase Y385F mutant complexed with 3,4-dihydroxybenzoate
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-DHB:
3,4-DIHYDROXYBENZOIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-P33:
3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL / precipitant*YM

ChemComp-BR:
BROMIDE ION

ChemComp-HOH:
WATER

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsOXIDOREDUCTASE / Aromatic compound hydroxylase / flavin / FAD

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