1jsc
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(New page: 200px<br /><applet load="1jsc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jsc, resolution 2.6Å" /> '''Crystal Structure of ...)
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Revision as of 16:25, 20 November 2007
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Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors
Overview
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.
About this Structure
1JSC is a Single protein structure of sequence from Saccharomyces cerevisiae with K, MG, 2HP, TPP and FAD as ligands. Active as Acetolactate synthase, with EC number 2.2.1.6 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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