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Protein Science (2001), 10:638-648.
Copyright © 2001 The Protein Society

Crystal structure of threonine synthase from Arabidopsis thaliana

Karine Thomazeau1, Gilles Curien2, Renaud Dumas2 and Valérie Biou1

1 Institut de Biologie Structurale Jean-Pierre Ebel, Unité Mixte de Recherche 5075 Centre National de la Recherche Scientifique-Centre d'Études Nucléaires-Université Joseph Fourier, F-38027 Grenoble, France
2 Unité Mixte de Recherche 1932 Centre National de la Recherche Scientifique-Institut National de la Recherche Agronomique-Aventis CropScience, F-69263 Lyon cedex 9, France

Reprint requests to: Valérie Biou, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075 CNRS-CEA-Université Joseph Fourier, F-38027 Grenoble, France; e-mail: biou{at}ibs.fr; fax: 33-476-88-54-94 or Renaud Dumas, UMR 1932 CNRS-INRA-Aventis CropScience, 14-20 rue Pierre Baizet, F-69263 Lyon cedex 9, France.

Threonine synthase (TS) is a PLP-dependent enzyme that catalyzes the last reaction in the synthesis of threonine from aspartate. In plants, the methionine pathway shares the same substrate, O-phospho-L-homoserine (OPH), and TS is activated by S-adenosyl-methionine (SAM), a downstream product of methionine synthesis. This positive allosteric effect triggered by the product of another pathway is specific to plants. The crystal structure of Arabidopsis thaliana apo threonine synthase was solved at 2.25 Å resolution from triclinic crystals using MAD data from the selenomethionated protein. The structure reveals a four-domain dimer with a two-stranded ß-sheet arm protruding from one monomer onto the other. This domain swap could form a lever through which the allosteric effect is transmitted. The N-terminal domain (domain 1) has a unique fold and is partially disordered, whereas the structural core (domains 2 and 3) shares the functional domain of PLP enzymes of the same family. It also has similarities with SAM-dependent methyltransferases. Structure comparisons allowed us to propose potential sites for pyridoxal-phosphate and SAM binding on TS; they are close to regions that are disordered in the absence of these molecules.

Keywords: Allostery; MAD; pyridoxal phosphate; S-adenosyl-methionine; threonine synthesis

Abbreviations: TS, threonine synthase • PLP, pyridoxal 5`-phosphate • OPH, O-phospho-L-homoserine • SAM, S-adenosyl-methionine • MAD, multiple wavelength anomalous dispersion • DTT, dithiothreitol • CGS, cystathionine-{gamma}-synthase • TD, threonine deaminase • CBS, cystathionine-ß-synthase • EC, enzyme classification


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