1AD3

CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE

Summary for 1AD3

• Entry DOI: 10.2210/pdb1ad3/pdb
• Descriptor: ALDEHYDE DEHYDROGENASE (CLASS 3), NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: nadp, oxidoreductase, aromatic aldehyde
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P11883
• Total number of polymer chains: 2
• Total formula weight: 101953.73

Authors

Liu, Z.-J.,Rose, J.,Wang, B.C. (deposition date: 1996-06-25, release date: 1997-07-07, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)