1od4
From Proteopedia
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| , resolution 2.7Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Acetyl-CoA carboxylase, with EC number 6.4.1.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1OD4 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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
Page seeded by OCA on Sun Mar 30 22:43:34 2008
