2c2g: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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 binding triggers a large reorganization of active site loops, in one monomer of the structural dimer and allows the displacement of PLP, to its active conformation. Comparison with other TS structures shows that, activation of the second monomer may be triggered by substrate binding., This structure also discloses a novel fold for two AdoMet binding sites, located at the dimer interface, each site containing two AdoMet effectors, bound in tandem. Moreover, aTS-AdoMet is the first structure of an enzyme, that uses AdoMet as an allosteric effector. | ||
==About this Structure== | ==About this Structure== | ||
2C2G is a | 2C2G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Active as [http://en.wikipedia.org/wiki/Threonine_synthase Threonine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.1 4.2.3.1] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C2G OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
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Revision as of 13:41, 5 November 2007
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CRYSTAL STRUCTURE OF THREONINE SYNTHASE FROM ARABIDOPSIS THALIANA IN COMPLEX WITH ITS COFACTOR PYRIDOXAL PHOSPHATE
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 binding triggers a large reorganization of active site loops, in one monomer of the structural dimer and allows the displacement of PLP, to its active conformation. Comparison with other TS structures shows that, activation of the second monomer may be triggered by substrate binding., This structure also discloses a novel fold for two AdoMet binding sites, located at the dimer interface, each site containing two AdoMet effectors, bound in tandem. Moreover, aTS-AdoMet is the first structure of an enzyme, that uses AdoMet as an allosteric effector.
About this StructureAbout this Structure
2C2G is a Single protein structure of sequence from Arabidopsis thaliana. Active as Threonine synthase, with EC number 4.2.3.1 Structure known Active Site: AC1. 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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