Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7KC2

Symmetry in Yeast Alcohol Dehydrogenase 1 -Closed Form with NADH

7KC2 の概要
エントリーDOI10.2210/pdb7kc2/pdb
関連するPDBエントリー4W6Z 5ENV
EMDBエントリー22805
分子名称Alcohol dehydrogenase, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
機能のキーワードalcohol dehydrogenase, nadh complex, 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150176.27
構造登録者
Subramanian, R.,Chang, L.,Li, Z.,Plapp, B.V. (登録日: 2020-10-04, 公開日: 2021-03-31, 最終更新日: 2024-10-23)
主引用文献Guntupalli, S.R.,Li, Z.,Chang, L.,Plapp, B.V.,Subramanian, R.
Cryo-Electron Microscopy Structures of Yeast Alcohol Dehydrogenase.
Biochemistry, 60:663-677, 2021
Cited by
PubMed Abstract: Structures of yeast alcohol dehydrogenase determined by X-ray crystallography show that the subunits have two different conformational states in each of the two dimers that form the tetramer. Apoenzyme and holoenzyme complexes relevant to the catalytic mechanism were described, but the asymmetry led to questions about the cooperativity of the subunits in catalysis. This study used cryo-electron microscopy (cryo-EM) to provide structures for the apoenzyme, two different binary complexes with NADH, and a ternary complex with NAD and 2,2,2-trifluoroethanol. All four subunits in each of these complexes are identical, as the tetramers have 2 symmetry, suggesting that there is no preexisting asymmetry and that the subunits can be independently active. The apoenzyme and one enzyme-NADH complex have "open" conformations and the inverted coordination of the catalytic zinc with Cys-43, His-66, Glu-67, and Cys-153, whereas another enzyme-NADH complex and the ternary complex have closed conformations with the classical coordination of the zinc with Cys-43, His-66, Cys-153, and a water or the oxygen of trifluoroethanol. The conformational change involves interactions of Arg-340 with the pyrophosphate group of the coenzyme and Glu-67. The cryo-EM and X-ray crystallography studies provide structures relevant for the catalytic mechanism.
PubMed: 33620215
DOI: 10.1021/acs.biochem.0c00921
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.67 Å)
構造検証レポート
Validation report summary of 7kc2
検証レポート(詳細版)ダウンロードをダウンロード

248942

件を2026-02-11に公開中

PDB statisticsPDBj update infoContact PDBjnumon