1e5x

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[[Image:1e5x.gif|left|200px]]
[[Image:1e5x.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1e5x |SIZE=350|CAPTION= <scene name='initialview01'>1e5x</scene>, resolution 2.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1e5x", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=MSO:SELENOMETHIONINE+SELENOXIDE'>MSO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= NUCLEAR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
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-->
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|DOMAIN=
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{{STRUCTURE_1e5x| PDB=1e5x | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5x OCA], [http://www.ebi.ac.uk/pdbsum/1e5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e5x RCSB]</span>
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}}
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'''STRUCTURE OF THREONINE SYNTHASE FROM ARABIDOPSIS THALIANA'''
'''STRUCTURE OF THREONINE SYNTHASE FROM ARABIDOPSIS THALIANA'''
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[[Category: Dumas, R.]]
[[Category: Dumas, R.]]
[[Category: Thomazeau, K.]]
[[Category: Thomazeau, K.]]
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[[Category: allostery]]
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[[Category: Allostery]]
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[[Category: plp enzyme]]
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[[Category: Plp enzyme]]
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[[Category: s-adenosyl-methionine]]
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[[Category: S-adenosyl-methionine]]
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[[Category: threonine biosynthesis]]
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[[Category: Threonine biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:45 2008''
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Revision as of 11:42, 2 May 2008

Image:1e5x.gif

Template:STRUCTURE 1e5x

STRUCTURE OF THREONINE SYNTHASE FROM ARABIDOPSIS THALIANA


Overview

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.

About this Structure

1E5X is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Crystal structure of threonine synthase from Arabidopsis thaliana., Thomazeau K, Curien G, Dumas R, Biou V, Protein Sci. 2001 Mar;10(3):638-48. PMID:11344332 Page seeded by OCA on Fri May 2 14:42:18 2008

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