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4.2.3.1: threonine synthase

This is an abbreviated version!
For detailed information about threonine synthase, go to the full flat file.

Word Map on EC 4.2.3.1

Reaction

O-phospho-L-homoserine
+
H2O
=
L-threonine
 +
phosphate

Synonyms

EC 4.2.99.2, MtTS, synthase, threonine, THR4, threonine synthase, threonine synthase (gene MA1610), threonine synthetase, ThrS, TS

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.1 threonine synthase

Crystallization

Crystallization on EC 4.2.3.1 - threonine synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallographic structure of Arabidopsis thaliana threonine synthase in complex with pyridoxal phosphate and with pyridoxal phosphate and S-adenosylmethionine
hanging drop method, 4°C, pH 6.5, resolution of 2.6 A
hanging-drop vapour-diffusion method at 293 K. Selenomethionine-substituted apo threonine synthase, 14 Met residues in 58000 Da
-
hanging-drop vapour-diffusion method, crystal structure of apo threonine synthase as solved at 2.25 A resolution from triclinic crystals
x-ray diffraction studies
-
refined to 2.5 A. The structure of MtTS has a homodimeric organization in which the two subunits are related by a non-crystallographic 2fold axis. Each subunit is composed of three domains
sitting-drop vapour-diffusion method, crystal structure at 2.7 A resolution
-
apo-protein and in complex with 2-amino-5-phosphonopentanoic acid and with (E)-4-(3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)-2-oxobut-3-enoic acid. The enzyme does not undergo any global conformational change upon the binding of pyridoxal 5'-phosphate. The binding of the substrate analog 2-amino-5-phosphonopentanoic acid to the holoenzyme induces a large conformational change from the open to the closed form in which the small domain moves as a rigid body to close the active site. This closed structure is maintained in the complex with (E)-4-(3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)-2-oxobut-3-enoic acid, indicating that threonine synthase is in the closed form in the enamine and the pyridoxal 5'-phosphate-alpha-aminocrotonate aldimine intermediates
comparative QM/MM calculations. The base that abstracts a proton from the attacking water is the epsilon-amino group of Lys61 rather than the phosphate ion. The phosphate ion is important for stabilizing the transition state of the normal transaldimination to form L-threonine by making a hydrogen bond with the hydroxy group of the L-threonine moiety. Proposal of a mechanism, in which a proton temporarily resides at the phenolate O3' of pyridoxal-5'-phosphate, for the transaldimination process
-
hanging drop vapour diffusion method at 293 K, unligated enzyme form and complex with substrate analogue 2-amino-5-phosphonopentanoic acid, structure determined at 2.15 A and 2.0 A resolution
-