1jsc

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{{STRUCTURE_1jsc| PDB=1jsc | SCENE= }}
{{STRUCTURE_1jsc| PDB=1jsc | SCENE= }}
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'''Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors'''
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===Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors===
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==Overview==
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Acetohydroxyacid synthase (AHAS; EC 4.1.3.18) catalyzes the first step in branched-chain amino acid biosynthesis. The enzyme requires thiamin diphosphate and FAD for activity, but the latter is unexpected, because the reaction involves no oxidation or reduction. Due to its presence in plants, AHAS is a target for sulfonylurea and imidazolinone herbicides. Here, the crystal structure to 2.6 A resolution of the catalytic subunit of yeast AHAS is reported. The active site is located at the dimer interface and is near the proposed herbicide-binding site. The conformation of FAD and its position in the active site are defined. The structure of AHAS provides a starting point for the rational design of new herbicides.
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(as it appears on PubMed at http://www.pubmed.gov), where 11902841 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11902841}}
==About this Structure==
==About this Structure==
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[[Category: Herbicide inhibition]]
[[Category: Herbicide inhibition]]
[[Category: Thiamin diphosphate]]
[[Category: Thiamin diphosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:49:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:43:47 2008''

Revision as of 17:43, 1 July 2008

Image:1jsc.png

Template:STRUCTURE 1jsc

Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors

Template:ABSTRACT PUBMED 11902841

About this Structure

1JSC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors., Pang SS, Duggleby RG, Guddat LW, J Mol Biol. 2002 Mar 22;317(2):249-62. PMID:11902841

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