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 2.6&Aring;" /> '''Crystal Structure of ...)
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[[Image:1jsc.gif|left|200px]]<br /><applet load="1jsc" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1jsc, resolution 2.6&Aring;" />
'''Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors'''<br />
'''Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors'''<br />
==Overview==
==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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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==
==About this Structure==
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1JSC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with K, MG, 2HP, TPP and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetolactate_synthase Acetolactate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.6 2.2.1.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JSC OCA].
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1JSC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=2HP:'>2HP</scene>, <scene name='pdbligand=TPP:'>TPP</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetolactate_synthase Acetolactate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.6 2.2.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JSC OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Duggleby, R.G.]]
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[[Category: Duggleby, R G.]]
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[[Category: Guddat, L.W.]]
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[[Category: Guddat, L W.]]
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[[Category: Pang, S.S.]]
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[[Category: Pang, S S.]]
[[Category: 2HP]]
[[Category: 2HP]]
[[Category: FAD]]
[[Category: FAD]]
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[[Category: thiamin diphosphate]]
[[Category: thiamin diphosphate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:32:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:11 2008''

Revision as of 11:26, 21 February 2008


1jsc, resolution 2.6Å

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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 , , , and 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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