2J6X : The crystal structure of lactate oxidase

  • Ingar Leiros (Bidrager)
  • Ellen Wang (Bidrager)
  • Tonni Rasmussen (Bidrager)
  • Esko Oksanen (Bidrager)
  • Heidi Repo (Bidrager)
  • Steffen Petersen (Bidrager)
  • Pirkko Heikinheimo (Bidrager)
  • Edward Hough (Bidrager)



Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.1 Classification:OXIDOREDUCTASE Release Date:2006-10-23 Deposition Date:2006-10-05 Revision Date:2011-05-08#2011-07-13 Molecular Weight:330986.28 Macromolecule Type:Protein Residue Count:2992 Atom Site Count:22565 DOI:10.2210/pdb2j6x/pdb 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.
Dato for tilgængelighed2006