 |
PDBsum entry 1gal
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase(flavoprotein)
|
PDB id
|
|
|
|
1gal
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of glucose oxidase from aspergillus niger refined at 2.3 a resolution.
|
|
|
Authors
|
|
H.J.Hecht,
H.M.Kalisz,
J.Hendle,
R.D.Schmid,
D.Schomburg.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
229,
153-172.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Glucose oxidase (beta-D-glucose: oxygen 1-oxidoreductase, EC 1.1.3.4) is an
FAD-dependent enzyme that catalyzes the oxidation of beta-D-glucose by molecular
oxygen. The crystal structure of the partially deglycosylated enzyme from
Aspergillus niger has been determined by isomorphous replacement and refined to
2.3 A resolution. The final crystallographic R-value is 18.1% for reflections
between 10.0 and 2.3 A resolution. The refined model includes 580 amino acid
residues, the FAD cofactor, six N-acetylglucosamine residues, three mannose
residues and 152 solvent molecules. The FAD-binding domain is topologically very
similar to other FAD-binding proteins. The substrate-binding domain is formed
from non-continuous segments of sequence and is characterized by a deep pocket.
One side of this pocket is formed by a six-stranded antiparallel beta-sheet with
the flavin ring system of FAD located at the bottom of the pocket on the
opposite side. Part of the entrance to the active site pocket is at the
interface to the second subunit of the dimeric enzyme and is formed by a
20-residue lid, which in addition covers parts of the FAD-binding site. The
carbohydrate moiety attached to Asn89 at the tip of this lid forms a link
between the subunits of the dimer.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Effects of carbohydrate depletion on the structure, Stability and activity of glucose oxidase from aspergillus niger.
|
|
|
Authors
|
|
H.M.Kalisz,
H.J.Hecht,
D.Schomburg,
R.D.Schmid.
|
|
|
Ref.
|
|
Biochim Biophys Acta, 1991,
1080,
138-142.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
