2J6X

The crystal structure of lactate oxidase

Summary for 2J6X

• Entry DOI: 10.2210/pdb2j6x/pdb
• Descriptor: LACTATE OXIDASE, FLAVIN MONONUCLEOTIDE, ZINC ION, ... (4 entities in total)
• Functional Keywords: biosensors, flavoenzyme, fmn-dependent, oxidoreductase
• Biological source: AEROCOCCUS VIRIDANS
• Total number of polymer chains: 8
• Total formula weight: 330986.29

Authors

Leiros, I.,Wang, E.,Rasmussen, T.,Oksanen, E.,Repo, H.,Petersen, S.B.,Heikinheimo, P.,Hough, E. (deposition date: 2006-10-05, release date: 2006-10-23, Last modification date: 2023-12-13)

Primary citation

Leiros, I.,Wang, E.,Rasmussen, T.,Oksanen, E.,Repo, H.,Petersen, S.B.,Heikinheimo, P.,Hough, E.
The 2.1 A Structure of Aerococcus Viridans L-Lactate Oxidase (Lox).
Acta Crystallogr.,Sect.F, 62:1185-, 2006

PubMed Abstract: 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.

PubMed: 17142893
DOI: 10.1107/S1744309106044678

Experimental method

X-RAY DIFFRACTION (2.1 Å)