1uyv
ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN L1705I/ V1967I MUTANT
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OverviewOverview
Acetyl-CoA carboxylases (ACCs) are crucial for the metabolism of fatty, acids, making these enzymes important targets for the development of, therapeutics against obesity, diabetes, and other diseases. The, carboxyltransferase (CT) domain of ACC is the site of action of commercial, herbicides, such as haloxyfop, diclofop, and sethoxydim. We have, determined the crystal structures at up to 2.5-A resolution of the CT, domain of yeast ACC in complex with the herbicide haloxyfop or diclofop., The inhibitors are bound in the active site, at the interface of the dimer, of the CT domain. Unexpectedly, inhibitor binding requires large, conformational changes for several residues in this interface, which, create a highly conserved hydrophobic pocket that extends deeply into the, core of the dimer. Two residues that affect herbicide sensitivity are, located in this binding site, and mutation of these residues disrupts the, structure of the domain. Other residues in the binding site are strictly, conserved among the CT domains.
About this StructureAbout this Structure
1UYV is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Acetyl-CoA carboxylase, with EC number 6.4.1.2 Full crystallographic information is available from OCA.
ReferenceReference
Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop., Zhang H, Tweel B, Tong L, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5910-5. Epub 2004 Apr 12. PMID:15079078
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