2j6x

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2j6x, resolution 2.10Å

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THE CRYSTAL STRUCTURE OF LACTATE OXIDASE

Overview

The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 A resolution. LOX catalyzes the flavin mononucleotide (FMN) dependent oxidation of lactate to pyruvate and hydrogen peroxide. LOX belongs to the alpha-hydroxy-acid oxidase flavoenzyme family; members of which bind similar substrates and to some extent have conserved catalytic properties and structural motifs. LOX crystallized as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. The present structure shows a conserved FMN coordination, but also reveals novel residues involved in substrate binding compared with other family members.

About this Structure

2J6X is a Single protein structure of sequence from Aerococcus viridans with and as ligands. Active as Transferred entry: 1.13.12.4, with EC number 1.1.3.2 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX)., Leiros I, Wang E, Rasmussen T, Oksanen E, Repo H, Petersen SB, Heikinheimo P, Hough E, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1185-90. Epub 2006 Nov 4. PMID:17142893

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