Summary for 4W6Z
| Entry DOI | 10.2210/pdb4w6z/pdb |
| Descriptor | Alcohol dehydrogenase 1, ZINC ION, NICOTINAMIDE-8-IODO-ADENINE-DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | tetramer of asymmetric dimers, zinc coordination, intramolecular disulfide bonds, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 149543.72 |
| Authors | plapp, B.v.,savarimuthu, b.r.,ramaswamy, s. (deposition date: 2014-08-21, release date: 2014-09-03, Last modification date: 2024-11-20) |
| Primary citation | Raj, S.B.,Ramaswamy, S.,Plapp, B.V. Yeast alcohol dehydrogenase structure and catalysis. Biochemistry, 53:5791-5803, 2014 Cited by PubMed Abstract: Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray crystallography at 2.4 Å resolution. The asymmetric unit contains four different subunits, arranged as similar dimers named AB and CD. The unit cell contains two different tetramers made up of "back-to-back" dimers, AB:AB and CD:CD. The A and C subunits in each dimer are structurally similar, with a closed conformation, bound coenzyme, and the oxygen of 2,2,2-trifluoroethanol ligated to the catalytic zinc in the classical tetrahedral coordination with Cys-43, Cys-153, and His-66. In contrast, the B and D subunits have an open conformation with no bound coenzyme, and the catalytic zinc has an alternative, inverted coordination with Cys-43, Cys-153, His-66, and the carboxylate of Glu-67. The asymmetry in the dimeric subunits of the tetramer provides two structures that appear to be relevant for the catalytic mechanism. The alternative coordination of the zinc may represent an intermediate in the mechanism of displacement of the zinc-bound water with alcohol or aldehyde substrates. Substitution of Glu-67 with Gln-67 decreases the catalytic efficiency by 100-fold. Previous studies of structural modeling, evolutionary relationships, substrate specificity, chemical modification, and site-directed mutagenesis are interpreted more fully with the three-dimensional structure. PubMed: 25157460DOI: 10.1021/bi5006442 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
