PDBsum entry 1v5f

Oxidoreductase

PDB id: 1v5f

Contents

Protein chain

589 a.a. *

Ligands

SO4 ×4

FAD

TPP

Metals

_MG

Waters ×563

* Residue conservation analysis

PDB id:

1v5f

Name:

Oxidoreductase

Title:

Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans

Structure:

Pyruvate oxidase. Chain: a. Ec: 1.2.3.3

Source:

Aerococcus viridans. Organism_taxid: 1377

Biol. unit:

Tetramer (from PDB file)

Resolution:

1.80Å R-factor: 0.161 R-free: 0.194

Authors:

M.T.Hossain,K.Suzuki,T.Yamamoto,S.Imamura,T.Sekiguchi,A.Takenaka

Key ref:

E.C.Juan et al. (2007). 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 Struct Biol Cryst Commun, 63, 900-907. PubMed id: 18007037

Date:

22-Nov-03 Release date: 28-Jun-05

Protein chain

No UniProt id for this chain

Struc: 589 a.a.

Acta Crystallogr Sect F Struct Biol Cryst Commun 63:900-907 (2007)

PubMed id: 18007037

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.

E.C.Juan, M.M.Hoque, M.T.Hossain, T.Yamamoto, S.Imamura, K.Suzuki, T.Sekiguchi, A.Takénaka.

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.