1ad3: Difference between revisions

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==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Liu, Z.J.]]
[[Category: Liu, Z J.]]
[[Category: Rose, J.]]
[[Category: Rose, J.]]
[[Category: Wang, B.C.]]
[[Category: Wang, B C.]]
[[Category: NAD]]
[[Category: NAD]]
[[Category: aromatic aldehyde]]
[[Category: aromatic aldehyde]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]


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