1ad3

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==Overview==
==Overview==
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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.
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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]]
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[[Category: Liu, Z.J.]]
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[[Category: Liu, Z J.]]
[[Category: Rose, J.]]
[[Category: Rose, J.]]
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[[Category: Wang, B.C.]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:29:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:15 2008''

Revision as of 09:43, 21 February 2008


1ad3, resolution 2.6Å

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CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE

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.

About this Structure

1AD3 is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Aldehyde dehydrogenase (NAD(P)(+)), with EC number 1.2.1.5 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

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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