1V5F

Crystal Structure of Pyruvate oxidase complexed with FAD and TPP, from Aerococcus viridans

Summary for 1V5F

• Entry DOI: 10.2210/pdb1v5f/pdb
• Related: 1POX 1V5E 1V5G
• Descriptor: Pyruvate oxidase, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, flavoprotein
• Biological source: Aerococcus viridans
• Total number of polymer chains: 1
• Total formula weight: 66855.83

Authors

Hossain, M.T.,Suzuki, K.,Yamamoto, T.,Imamura, S.,Sekiguchi, T.,Takenaka, A. (deposition date: 2003-11-22, release date: 2005-06-28, Last modification date: 2023-10-25)

Primary citation

Juan, E.C.,Hoque, M.M.,Hossain, M.T.,Yamamoto, T.,Imamura, S.,Suzuki, K.,Sekiguchi, T.,Takenaka, A.
The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis.
Acta Crystallogr.,Sect.F, 63:900-907, 2007

PubMed Abstract: The crystal structures of pyruvate oxidase from Aerococcus viridans (AvPOX) complexed with flavin adenine dinucleotide (FAD), with FAD and thiamine diphosphate (ThDP) and with FAD and the 2-acetyl-ThDP intermediate (AcThDP) have been determined at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric AvPOX enzyme consists of three domains, as observed in other ThDP-dependent enzymes. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while ThDP is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Of particular interest is the role of Lys478, the side chain of which may be bent or extended depending on the stage of catalysis. The structures also provide insight into the routes for electron transfer to FAD and the involvement of active-site residues in the catalysis of pyruvate to its products.

PubMed: 18007037
DOI: 10.1107/S1744309107041012

Experimental method

X-RAY DIFFRACTION (1.8 Å)