 |
PDBsum entry 1v5f
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
1v5f
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
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.
|
|
|
Authors
|
|
E.C.Juan,
M.M.Hoque,
M.T.Hossain,
T.Yamamoto,
S.Imamura,
K.Suzuki,
T.Sekiguchi,
A.Takénaka.
|
|
|
Ref.
|
|
Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007,
63,
900-907.
|
|
|
PubMed id
|
|
|
|
|
Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
|
|
|
|
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.
|
|
|
|
|
|
|
