 |
PDBsum entry 1wql
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
1wql
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of the terminal oxygenase component of cumene dioxygenase from pseudomonas fluorescens ip01.
|
|
|
Authors
|
|
X.Dong,
S.Fushinobu,
E.Fukuda,
T.Terada,
S.Nakamura,
K.Shimizu,
H.Nojiri,
T.Omori,
H.Shoun,
T.Wakagi.
|
|
|
Ref.
|
|
J Bacteriol, 2005,
187,
2483-2490.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The crystal structure of the terminal component of the cumene dioxygenase
multicomponent enzyme system of Pseudomonas fluorescens IP01 (CumDO) was
determined at a resolution of 2.2 A by means of molecular replacement by using
the crystal structure of the terminal oxygenase component of naphthalene
dioxygenase from Pseudomonas sp. strain NCIB 9816-4 (NphDO). The ligation of the
two catalytic centers of CumDO (i.e., the nonheme iron and Rieske [2Fe-2S]
centers) and the bridging between them in neighboring catalytic subunits by
hydrogen bonds through a single amino acid residue, Asp231, are similar to those
of NphDO. An unidentified external ligand, possibly dioxygen, was bound at the
active site nonheme iron. The entrance to the active site of CumDO is different
from the entrance to the active site of NphDO, as the two loops forming the lid
exhibit great deviation. On the basis of the complex structure of NphDO, a
biphenyl substrate was modeled in the substrate-binding pocket of CumDO. The
residues surrounding the modeled biphenyl molecule include residues that have
already been shown to be important for its substrate specificity by a number of
engineering studies of biphenyl dioxygenases.
|
|
|
|
|
|
|
