1f14

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spinqualitylabelsall models 1f14, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

L-3-HYDROXYACYL-COA DEHYDROGENASE (APO)

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

l-3-Hydroxyacyl-CoA dehydrogenase reversibly catalyzes the conversion of, l-3-hydroxyacyl-CoA to 3-ketoacyl-CoA concomitant with the reduction of, NAD(+) to NADH as part of the beta-oxidation spiral. In this report, crystal structures have been solved for the apoenzyme, binary complexes of, the enzyme with reduced cofactor or 3-hydroxybutyryl-CoA substrate, and an, abortive ternary complex of the enzyme with NAD(+) and acetoacetyl-CoA., The models illustrate positioning of cofactor and substrate within the, active site of the enzyme. Comparison of these structures with the, previous model of the enzyme-NAD(+) complex reveals that although, significant shifting of the NAD(+)-binding domain relative to the, C-terminal domain occurs in the ternary and substrate-bound complexes, there are few differences between the apoenzyme and cofactor-bound, complexes. Analysis of these models clarifies the role of key amino acids, implicated in catalysis and highlights additional critical residues., Furthermore, a novel charge transfer complex has been identified in the, course of abortive ternary complex formation, and its characterization, provides additional insight into aspects of the catalytic mechanism of, l-3-hydroxyacyl-CoA dehydrogenase.

Disease

Known diseases associated with this structure: 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency OMIM:[300256], 3-hydroxyacyl-CoA dehydrogenase deficiency OMIM:[601609], Hyperinsulinemic hypoglycemia, familial, 4 OMIM:[601609]

About this Structure

1F14 is a Single protein structure of sequence from Homo sapiens. Active as 3-hydroxyacyl-CoA dehydrogenase, with EC number 1.1.1.35 Full crystallographic information is available from OCA.

Reference

Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase., Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ, J Biol Chem. 2000 Sep 1;275(35):27186-96. PMID:10840044

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