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Year: 2001 Volume: 10 Issue: 2

Year: 2001 Volume: 10 Issue: 1

Crystal structure of threonine synthase from Arabidopsis thaliana.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Curien, G. Biou, V. Thomazeau, K. Dumas, R.
Description	Country affiliation: France Author Affiliation: Thomazeau K ( Institut de Biologie Structurale Jean-Pierre Ebel, Unité Mixte de Recherche 5075 Centre National de la Recherche Scientifique-Centre d'Etudes Nucléaires-Université Joseph Fourier, F-38027 Grenoble, France.)
Abstract	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 A resolution from triclinic crystals using MAD data from the selenomethionated protein. The structure reveals a four-domain dimer with a two-stranded beta-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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carbon-oxygen Lyases Chemistry Metabolism Pyridoxal Phosphate S-adenosylmethionine Amino Acid Sequence Arabidopsis Enzymology Binding Sites Conserved Sequence Crystallography Enzyme Activation Molecular Sequence Data Oxidation-reduction Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary Comparative Study Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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