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Liu ZJ, et al.  (1997) The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. Nat Struct Biol 4(4):317-26

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.

Status: Published

Type: Journal Article

PubMed ID: 9095201

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Liu ZJ Sun YJ Rose J Chung YJ Hsiao CD Chang WR Kuo I Perozich J Lindahl R Hempel J Wang BC Papers in SGD Colleagues in SGD PubMed Google Scholar

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