1jsc
From Proteopedia
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|PDB= 1jsc |SIZE=350|CAPTION= <scene name='initialview01'>1jsc</scene>, resolution 2.6Å | |PDB= 1jsc |SIZE=350|CAPTION= <scene name='initialview01'>1jsc</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=2HP:DIHYDROGENPHOSPHATE+ION'>2HP</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= ILV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= ILV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jsc OCA], [http://www.ebi.ac.uk/pdbsum/1jsc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jsc RCSB]</span> | ||
}} | }} | ||
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[[Category: Guddat, L W.]] | [[Category: Guddat, L W.]] | ||
[[Category: Pang, S S.]] | [[Category: Pang, S S.]] | ||
| - | [[Category: 2HP]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: K]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: TPP]] | ||
[[Category: acetohydroxyacid synthase]] | [[Category: acetohydroxyacid synthase]] | ||
[[Category: acetolactate synthase]] | [[Category: acetolactate synthase]] | ||
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[[Category: thiamin diphosphate]] | [[Category: thiamin diphosphate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:16 2008'' |
Revision as of 18:38, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | ILV2 (Saccharomyces cerevisiae) | ||||||
| Activity: | Acetolactate synthase, with EC number 2.2.1.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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