We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1yi1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yi1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1yi1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yi1| PDB=1yi1 | SCENE= }}
{{STRUCTURE_1yi1| PDB=1yi1 | SCENE= }}
-
'''Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Tribenuron methyl'''
+
===Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Tribenuron methyl===
-
==Overview==
+
<!--
-
The sulfonylureas and imidazolinones are potent commercial herbicide families. They are among the most popular choices for farmers worldwide, because they are nontoxic to animals and highly selective. These herbicides inhibit branched-chain amino acid biosynthesis in plants by targeting acetohydroxyacid synthase (AHAS, EC 2.2.1.6). This report describes the 3D structure of Arabidopsis thaliana AHAS in complex with five sulfonylureas (to 2.5 A resolution) and with the imidazolinone, imazaquin (IQ; 2.8 A). Neither class of molecule has a structure that mimics the substrates for the enzyme, but both inhibit by blocking a channel through which access to the active site is gained. The sulfonylureas approach within 5 A of the catalytic center, which is the C2 atom of the cofactor thiamin diphosphate, whereas IQ is at least 7 A from this atom. Ten of the amino acid residues that bind the sulfonylureas also bind IQ. Six additional residues interact only with the sulfonylureas, whereas there are two residues that bind IQ but not the sulfonylureas. Thus, the two classes of inhibitor occupy partially overlapping sites but adopt different modes of binding. The increasing emergence of resistant weeds due to the appearance of mutations that interfere with the inhibition of AHAS is now a worldwide problem. The structures described here provide a rational molecular basis for understanding these mutations, thus allowing more sophisticated AHAS inhibitors to be developed. There is no previously described structure for any plant protein in complex with a commercial herbicide.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16407096}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16407096 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16407096}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Thiamin diphosphate]]
[[Category: Thiamin diphosphate]]
[[Category: Tribenuron methyl]]
[[Category: Tribenuron methyl]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:20:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:48:41 2008''

Revision as of 02:48, 28 July 2008

Image:1yi1.png

Template:STRUCTURE 1yi1

Crystal structure of Arabidopsis thaliana Acetohydroxyacid synthase In Complex With A Sulfonylurea Herbicide, Tribenuron methyl

Template:ABSTRACT PUBMED 16407096

About this Structure

1YI1 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase., McCourt JA, Pang SS, King-Scott J, Guddat LW, Duggleby RG, Proc Natl Acad Sci U S A. 2006 Jan 17;103(3):569-73. Epub 2006 Jan 10. PMID:16407096

Page seeded by OCA on Mon Jul 28 05:48:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yi1"
Personal tools