Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution.
The conformation of the polypeptide chain in horse liver alcohol dehydrogenase (EC 1.1.1.1), as well as the binding sites for some inhibitor molecules, have been determined from x-ray crystallographic data to a resolution of 2.9 A. Each subunit of the dimeric molecule is organized into two parts unequal in size and separated by a wide and deep active-site cleft. The adenosine moiety of the coenzyme is bound within the smaller region. Interactions between these coenzyme-binding substructures define the subunit contact area of the molecule. The "catalytic" zinc atoms are bound at the bottom of the clefts about 20 A from the surface of the molecule. The coenzyme binding region has a main-chain conformation very similar to a corresponding region in lactate and malate dehydrogenase. It is suggested that this substructure is a general one for binding of nucleotides and, in particular, the coenzyme NAD(+).
D000429:Alcohol Oxidoreductases; D000818:Animals; D001665:Binding Sites; D006736:Horses; D008099:Liver / Q000201:enzymology*; D008961:Models, Structural; D009243:NAD; D011487:Protein Conformation; D014961:X-Ray Diffraction
D009243:NAD; D000429:Alcohol Oxidoreductases