1JSC

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

Summary for 1JSC

• Entry DOI: 10.2210/pdb1jsc/pdb
• Descriptor: ACETOHYDROXY-ACID SYNTHASE, POTASSIUM ION, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: acetohydroxyacid synthase, acetolactate synthase, fad, thiamin diphosphate, herbicide inhibition, lyase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Mitochondrion: P07342
• Total number of polymer chains: 2
• Total formula weight: 139745.49

Authors

Pang, S.S.,Duggleby, R.G.,Guddat, L.W. (deposition date: 2001-08-17, release date: 2002-01-16, Last modification date: 2023-08-16)

Primary citation

Pang, S.S.,Duggleby, R.G.,Guddat, L.W.
Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.
J.Mol.Biol., 317:249-262, 2002

PubMed Abstract: 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.

PubMed: 11902841
DOI: 10.1006/jmbi.2001.5419

Experimental method

X-RAY DIFFRACTION (2.6 Å)