1od2
From Proteopedia
(New page: 200px<br /> <applet load="1od2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1od2, resolution 2.7Å" /> '''ACETYL-COA CARBOXYLA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 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 ACO and ADE as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OD2 OCA]]. | + | 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 ACO and ADE 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OD2 OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12663926 12663926] | 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] | ||
| + | [[Category: Acetyl-CoA carboxylase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: obesity]] | [[Category: obesity]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:35:59 2007'' |
Revision as of 11:31, 30 October 2007
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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] with ACO and ADE as [ligands]. Active as [Acetyl-CoA carboxylase], with EC number [6.4.1.2]. Structure known Active Site: AC1. 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 Tue Oct 30 13:35:59 2007
Categories: Acetyl-CoA carboxylase | Saccharomyces cerevisiae | Single protein | Shen, Y. | Tong, L. | Yang, Z. | Zhang, H. | ACO | ADE | Acc | Acetyl-coa | Acetyl-coa carboxylase | Obesity
