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| [[Image:1uyv.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1uyv| PDB=1uyv | SCENE= }} | | {{STRUCTURE_1uyv| PDB=1uyv | SCENE= }} |
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| '''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN L1705I/ V1967I MUTANT'''
| | ===ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN L1705I/ V1967I MUTANT=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15079078}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15079078 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15079078}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Carboxyltransferase]] | | [[Category: Carboxyltransferase]] |
| [[Category: Mutant]] | | [[Category: Mutant]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:52:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:37:32 2008'' |