1AD3

CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE

1AD3 の概要

• エントリーDOI: 10.2210/pdb1ad3/pdb
• 分子名称: ALDEHYDE DEHYDROGENASE (CLASS 3), NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: nadp, oxidoreductase, aromatic aldehyde
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: P11883
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101953.73

構造登録者

Liu, Z.-J.,Rose, J.,Wang, B.C. (登録日: 1996-06-25, 公開日: 1997-07-07, 最終更新日: 2024-02-07)

主引用文献

Liu, Z.J.,Sun, Y.J.,Rose, J.,Chung, Y.J.,Hsiao, C.D.,Chang, W.R.,Kuo, I.,Perozich, J.,Lindahl, R.,Hempel, J.,Wang, B.C.
The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.
Nat.Struct.Biol., 4:317-326, 1997

PubMed Abstract: The first structure of an aldehyde dehydrogenase (ALDH) is described at 2.6 A resolution. Each subunit of the dimeric enzyme contains an NAD-binding domain, a catalytic domain and a bridging domain. At the interface of these domains is a 15 A long funnel-shaped passage with a 6 x 12 A opening leading to a putative catalytic pocket. A new mode of NAD binding, which differs substantially from the classic beta-alpha-beta binding mode associated with the 'Rossmann fold', is observed which we term the beta-alpha,beta mode. Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family. A mechanism for enzymatic specificity and activity is postulated.

PubMed: 9095201
DOI: 10.1038/nsb0497-317

実験手法

X-RAY DIFFRACTION (2.6 Å)