2E77
Crystal structure of L-lactate oxidase with pyruvate complex
Summary for 2E77
| Entry DOI | 10.2210/pdb2e77/pdb |
| Related | 2DU2 |
| Descriptor | Lactate oxidase, FLAVIN MONONUCLEOTIDE, PYRUVIC ACID, ... (4 entities in total) |
| Functional Keywords | tim barrel, fmn, oxidoreductase |
| Biological source | Aerococcus viridans |
| Total number of polymer chains | 4 |
| Total formula weight | 166012.97 |
| Authors | Morimoto, Y. (deposition date: 2007-01-06, release date: 2007-11-27, Last modification date: 2023-11-15) |
| Primary citation | Li, S.J.,Umena, Y.,Yorita, K.,Matsuoka, T.,Kita, A.,Fukui, K.,Morimoto, Y. Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution. Biochem.Biophys.Res.Commun., 358:1002-1007, 2007 Cited by PubMed Abstract: L-Lactate oxidase (LOX) from Aerococcus viridans catalyzes the oxidation of L-lactate to pyruvate by the molecular oxygen and belongs to a large family of 2-hydroxy acid-dependent flavoenzymes. To investigate the interaction of LOX with pyruvate in structural details and understand the chemical mechanism of flavin-dependent L-lactate dehydrogenation, the LOX-pyruvate complex was crystallized and the crystal structure of the complex has been solved at a resolution of 1.90 Angstrom. One pyruvate molecule bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit, were identified. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265. The alpha-carbon of pyruvate is found to be 3.13 Angstrom from the N5 atom of FMN at an angle of 105.4 degrees from the flavin N5-N10 axis. PubMed: 17517371DOI: 10.1016/j.bbrc.2007.05.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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