4W6Z

YEAST ALCOHOL DEHYDROGENASE I, SACCHAROMYCES CEREVISIAE FERMENTATIVE ENZYME

「2HCY」から置き換えられました

4W6Z の概要

• エントリーDOI: 10.2210/pdb4w6z/pdb
• 分子名称: Alcohol dehydrogenase 1, ZINC ION, NICOTINAMIDE-8-IODO-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: tetramer of asymmetric dimers, zinc coordination, intramolecular disulfide bonds, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 149543.72

構造登録者

plapp, B.v.,savarimuthu, b.r.,ramaswamy, s. (登録日: 2014-08-21, 公開日: 2014-09-03, 最終更新日: 2024-11-20)

主引用文献

Raj, S.B.,Ramaswamy, S.,Plapp, B.V.
Yeast alcohol dehydrogenase structure and catalysis.
Biochemistry, 53:5791-5803, 2014

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: 25157460
DOI: 10.1021/bi5006442

実験手法

X-RAY DIFFRACTION (2.4 Å)