1od2

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Revision as of 18:45, 29 October 2007

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spinqualitylabelsall models 1od2, resolution 2.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN

Overview

Acetyl-coenzyme A carboxylases (ACCs) are required for the biosynthesis, and oxidation of long-chain fatty acids. They are targets for therapeutics, against obesity and diabetes, and several herbicides function by, inhibiting their carboxyltransferase (CT) domain. We determined the, crystal structure of the free enzyme and the coenzyme A complex of yeast, CT at 2.7 angstrom resolution and found that it comprises two domains, both belonging to the crotonase/ClpP superfamily. The active site is at, the interface of a dimer. Mutagenesis and kinetic studies reveal the, functional roles of conserved residues here. The herbicides target the, active site of CT, providing a lead for inhibitor development against, human ACCs.

About this Structure

1OD2 is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with ACO and ADE as [ligands]. Active as [[1]], with EC number [6.4.1.2]. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase., Zhang H, Yang Z, Shen Y, Tong L, Science. 2003 Mar 28;299(5615):2064-7. PMID:12663926

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