1od4: Difference between revisions

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-[[Image:1od4.jpg|left|200px]]
+{{Seed}}
+[[Image:1od4.png|left|200px]]
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 {{STRUCTURE_1od4|  PDB=1od4  |  SCENE=  }}
-'''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12663926}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12663926 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12663926}}
 ==About this Structure==
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 [[Category: Ligase]]
 [[Category: Obesity]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:41:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:29:14 2008''