We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
1od2
From Proteopedia
Revision as of 14:39, 28 September 2014 by OCA (Talk | contribs)
1od2 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Zhang H, Yang Z, Shen Y, Tong L. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Science. 2003 Mar 28;299(5615):2064-7. PMID:12663926 doi:http://dx.doi.org/10.1126/science.1081366
