1uyr
From Proteopedia
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| - | [[Image:1uyr.gif|left|200px]] | + | [[Image:1uyr.gif|left|200px]] |
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| - | '''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN COMPLEX WITH INHIBITOR DICLOFOP''' | + | {{Structure |
| + | |PDB= 1uyr |SIZE=350|CAPTION= <scene name='initialview01'>1uyr</scene>, resolution 2.5Å | ||
| + | |SITE= <scene name='pdbsite=AC1:D1l+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=D1L:2-[4-(2,4-DICHLOROPHENOXY)PHENOXY]PROPANOIC ACID'>D1L</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN COMPLEX WITH INHIBITOR DICLOFOP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UYR is a [ | + | 1UYR 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=1UYR OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15079078 15079078] |
[[Category: Acetyl-CoA carboxylase]] | [[Category: Acetyl-CoA carboxylase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:38:38 2008'' |
Revision as of 12:38, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Acetyl-CoA carboxylase, with EC number 6.4.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN COMPLEX WITH INHIBITOR DICLOFOP
Overview
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 Structure
1UYR is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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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