2c2g
CRYSTAL STRUCTURE OF THREONINE SYNTHASE FROM ARABIDOPSIS THALIANA IN COMPLEX WITH ITS COFACTOR PYRIDOXAL PHOSPHATE
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OverviewOverview
Threonine synthase (TS) is a fold-type II pyridoxal phosphate, (PLP)-dependent enzyme that catalyzes the ultimate step of threonine, synthesis in plants and microorganisms. Unlike the enzyme from, microorganisms, plant TS is activated by S-adenosylmethionine (AdoMet)., The mechanism of activation has remained unknown up to now. We report here, the crystallographic structures of Arabidopsis thaliana TS in complex with, PLP (aTS) and with PLP and AdoMet (aTS-AdoMet), which show with atomic, detail how AdoMet activates TS. The aTS structure reveals a PLP, orientation never previously observed for a type II PLP-dependent enzyme, and explains the low activity of plant TS in the absence of its allosteric, activator. The aTS-AdoMet structure shows that activation of the enzyme, upon AdoMet ... [(full description)]
About this StructureAbout this Structure
2C2G is a [Single protein] structure of sequence from [Arabidopsis thaliana]. Active as [[1]], with EC number [4.2.3.1]. Full crystallographic information is available from [OCA].
ReferenceReference
Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site., Mas-Droux C, Biou V, Dumas R, J Biol Chem. 2006 Feb 24;281(8):5188-96. Epub 2005 Nov 29. PMID:16319072
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