The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold
The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold
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DOI：
10.1038/nsb0497-317
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发表时间：
1997-04-01
期刊：
影响因子：
--
通讯作者：
Wang, BC
中科院分区：
文献类型：
--
作者：
Liu, ZJ;Sun, YJ;Wang, BC
醛脱氢酶（ALDH）的第一结构以2.6埃分辨率描述。二聚体酶的每个亚基含有NAD结合结构域、催化结构域和桥接结构域。在这些结构域的界面处是15埃长的漏斗形通道，其具有6 X 12埃的开口，导致推定的催化口袋。观察到一种新的NAD结合模式，其与与“Rossmann折叠”相关的经典β-α-β结合模式有很大不同，我们称之为β-α，β模式。3类ALDH与其他ALDH的序列比较表明，类似的多肽折叠，新的NAD-结合模式和催化位点的这个家庭。推测了酶的特异性和活性的机制。
The first structure of an aldehyde dehydrogenase (ALDH) is described at 2.6 Angstrom 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 Angstrom long funnel-shaped passage with a 6 x 12 Angstrom 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.