1od4

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[[Image:1od4.jpg|left|200px]]
[[Image:1od4.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1od4 |SIZE=350|CAPTION= <scene name='initialview01'>1od4</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1od4", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Ade+Binding+Site+For+Chain+C'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1od4| PDB=1od4 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1od4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1od4 OCA], [http://www.ebi.ac.uk/pdbsum/1od4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1od4 RCSB]</span>
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}}
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'''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN'''
'''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN'''
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[[Category: Yang, Z.]]
[[Category: Yang, Z.]]
[[Category: Zhang, H.]]
[[Category: Zhang, H.]]
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[[Category: acc]]
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[[Category: Acc]]
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[[Category: acetyl-coa carboxylase]]
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[[Category: Acetyl-coa carboxylase]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: obesity]]
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[[Category: Obesity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:41:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:43:34 2008''
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Revision as of 00:41, 3 May 2008

Image:1od4.jpg

Template:STRUCTURE 1od4

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 Sat May 3 03:41:25 2008

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OCA

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