The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens.
The 1.94 A structure of methanol dehydrogenase has been used to provide a model structure for part of a membrane quinohaemoprotein alcohol dehydrogenase. The basic superbarrel structure and the active-site region are retained, indicating essentially similar mechanisms of action, but there are considerable differences in the external loops, particularly those involved in formation of the shallow funnel leading to the active site.
Cozier
G E
GE
SERC Centre for Molecular Recognition, Department of Biochemistry, University of Southampton, U.K.
Giles
I G
IG
Anthony
C
C
D000091:Acetobacter / Q000201:enzymology*; D000426:Alcohol Dehydrogenase / Q000648:ultrastructure*; D000429:Alcohol Oxidoreductases / Q000648:ultrastructure*; D000595:Amino Acid Sequence; D001665:Binding Sites; D016384:Consensus Sequence; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D045542:PQQ Cofactor; D017434:Protein Structure, Tertiary; D015363:Quinolones / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D015363:Quinolones; D045542:PQQ Cofactor; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C019641:alcohol dehydrogenase (acceptor)