1e6w

From Proteopedia

Revision as of 13:02, 30 October 2007

RAT BRAIN 3-HYDROXYACYL-COA DEHYDROGENASE BINARY COMPLEX WITH NADH AND ESTRADIOL

Overview

Human type II hydroxyacyl-CoA dehydrogenase/amyloid-beta binding alcohol, dehydrogenase (HADH II/ABAD) is an oxidoreductase whose salient features, include broad substrate specificity, encompassing 3-hydroxyacyl-CoA, derivatives, hydroxysteroids, alcohols and beta-hydroxybutyrate, and the, capacity to bind amyloid-beta peptide, leading to propagation of, amyloid-induced cell stress. In this study, we examine the structure and, enzymatic activity of the homologous rat HADH II/ABAD enzyme. We report, the crystal structure of rat HADH II/ABAD as a binary complex with its, NADH cofactor to 2.0 A resolution, as a ternary complex with NAD(+) and, 3-ketobutyrate (acetoacetate) to 1.4 A resolution, and as a ternary, complex with NADH and 17 beta-estradiol to 1.7 A resolution. This first, crystal ... [(full description)]

About this Structure

1E6W is a [Single protein] structure of sequence from [Rattus norvegicus] with NAD and EST as [ligands]. Active as [3-hydroxyacyl-CoA dehydrogenase], with EC number [1.1.1.35]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, ASA, ASB, ASC and ASD. Full crystallographic information is available from [OCA].

Reference

Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD)., Powell AJ, Read JA, Banfield MJ, Gunn-Moore F, Yan SD, Lustbader J, Stern AR, Stern DM, Brady RL, J Mol Biol. 2000 Oct 20;303(2):311-27. PMID:11023795

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