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Structure paper

TitleDynamic interactions in the l-lactate oxidase active site facilitate substrate binding at pH4.5.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 568, Page 131-135, Year 2021
Publish dateJun 10, 2021 (structure data deposition date)
AuthorsFurubayashi, N. / Inaka, K. / Kamo, M. / Umena, Y. / Matsuoka, T. / Morimoto, Y.
External linksBiochem. Biophys. Res. Commun. / PubMed:34214876
MethodsX-ray diffraction
Resolution1.3 - 1.41 Å
Structure data

PDB-7f1y:
L-lactate oxidase without substrate
Method: X-RAY DIFFRACTION / Resolution: 1.33 Å

PDB-7f20:
L-lactate oxidase with L-lactate
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-7f21:
L-lactate oxidase with D-lactate
Method: X-RAY DIFFRACTION / Resolution: 1.38 Å

PDB-7f22:
L-lactate oxidase with pyruvate
Method: X-RAY DIFFRACTION / Resolution: 1.41 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-2OP:
(2S)-2-HYDROXYPROPANOIC ACID

ChemComp-LAC:
LACTIC ACID

ChemComp-PYR:
PYRUVIC ACID

Source
  • aerococcus viridans (bacteria)
KeywordsOXIDOREDUCTASE / L-lactate / complex / D-lactate / pyruvate

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