1OD2

Acetyl-CoA Carboxylase Carboxyltransferase Domain

Summary for 1OD2

• Entry DOI: 10.2210/pdb1od2/pdb
• Related: 1OD4
• Descriptor: ACETYL-COENZYME A CARBOXYLASE, ACETYL COENZYME *A, ADENINE, ... (4 entities in total)
• Functional Keywords: ligase, acc, acetyl-coa, acetyl-coa carboxylase, obesity
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 2
• Total formula weight: 184931.54

Authors

Zhang, H.,Yang, Z.,Shen, Y.,Tong, L. (deposition date: 2003-02-12, release date: 2003-04-03, Last modification date: 2024-10-16)

Primary citation

Zhang, H.,Yang, Z.,Shen, Y.,Tong, L.
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
Science, 299:2064-2067, 2003

PubMed Abstract: 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.

PubMed: 12663926
DOI: 10.1126/science.1081366

Experimental method

X-RAY DIFFRACTION (2.7 Å)