1od2

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[[Image:1od2.jpg|left|200px]]<br /><applet load="1od2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1od2.jpg|left|200px]]
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caption="1od2, resolution 2.7&Aring;" />
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'''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN'''<br />
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{{Structure
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|PDB= 1od2 |SIZE=350|CAPTION= <scene name='initialview01'>1od2</scene>, resolution 2.7&Aring;
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|SITE= <scene name='pdbsite=AC1:Aco+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene> and <scene name='pdbligand=ADE:ADENINE'>ADE</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ACO:'>ACO</scene> and <scene name='pdbligand=ADE:'>ADE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Aco+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OD2 OCA].
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1OD2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OD2 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12663926 12663926]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12663926 12663926]
[[Category: Acetyl-CoA carboxylase]]
[[Category: Acetyl-CoA carboxylase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: obesity]]
[[Category: obesity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:07 2008''

Revision as of 11:09, 20 March 2008

Image:1od2.jpg


PDB ID 1od2

Drag the structure with the mouse to rotate
, resolution 2.7Å
Sites:
Ligands: and
Activity: Acetyl-CoA carboxylase, with EC number 6.4.1.2
Coordinates: save as pdb, mmCIF, xml



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

1OD2 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

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