2e77: Difference between revisions

Revision as of 18:06, 21 February 2008

Crystal structure of L-lactate oxidase with pyruvate complex

OverviewOverview

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.

About this StructureAbout this Structure

2E77 is a Single protein structure of sequence from Aerococcus viridans with and as ligands. Active as Lactate 2-monooxygenase, with EC number 1.13.12.4 Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic study on the interaction of L-lactate oxidase with pyruvate at 1.9 Angstrom resolution., Li SJ, Umena Y, Yorita K, Matsuoka T, Kita A, Fukui K, Morimoto Y, Biochem Biophys Res Commun. 2007 Jul 13;358(4):1002-7. Epub 2007 May 11. PMID:17517371

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 ==Overview==
-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.
+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.
 ==About this Structure==
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