1ad3
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CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE
OverviewOverview
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.
About this StructureAbout this Structure
1AD3 is a [Single protein] structure of sequence from [Rattus norvegicus] with NAD as [ligand]. Active as [Aldehyde dehydrogenase (NAD(P)(+))], with EC number [1.2.1.5]. Structure known Active Sites: CTA and CTB. Full crystallographic information is available from [OCA].
ReferenceReference
The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold., Liu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC, Nat Struct Biol. 1997 Apr;4(4):317-26. PMID:9095201
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