1uyv: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1uyv.gif|left|200px]] | [[Image:1uyv.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1uyv", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1uyv| PDB=1uyv | SCENE= }} | ||
}} | |||
'''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN L1705I/ V1967I MUTANT''' | '''ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN L1705I/ V1967I MUTANT''' | ||
| Line 29: | Line 26: | ||
[[Category: Tweel, B.]] | [[Category: Tweel, B.]] | ||
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: | [[Category: Carboxylase]] | ||
[[Category: | [[Category: Carboxyltransferase]] | ||
[[Category: | [[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 | |||
Revision as of 11:52, 3 May 2008
ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN L1705I/ V1967I MUTANT
OverviewOverview
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 StructureAbout this Structure
1UYV is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 11:52:49 2008