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1e5x

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(New page: 200px<br /><applet load="1e5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5x, resolution 2.25&Aring;" /> '''STRUCTURE OF THREONI...)
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[[Image:1e5x.gif|left|200px]]<br /><applet load="1e5x" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e5x, resolution 2.25&Aring;" />
 
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'''STRUCTURE OF THREONINE SYNTHASE FROM ARABIDOPSIS THALIANA'''<br />
 
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==Overview==
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==Structure of threonine synthase from Arabidopsis thaliana==
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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.
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<StructureSection load='1e5x' size='340' side='right'caption='[[1e5x]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1e5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5X FirstGlance]. <br>
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1E5X 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E5X OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=MSO:SELENOMETHIONINE+SELENOXIDE'>MSO</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5x OCA], [https://pdbe.org/1e5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5x RCSB], [https://www.ebi.ac.uk/pdbsum/1e5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5x ProSAT]</span></td></tr>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11344332 11344332]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THRC1_ARATH THRC1_ARATH] Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/1e5x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e5x ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Threonine synthase]]
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[[Category: Biou V]]
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[[Category: Biou, V.]]
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[[Category: Curien G]]
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[[Category: Curien, G.]]
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[[Category: Dumas R]]
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[[Category: Dumas, R.]]
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[[Category: Thomazeau K]]
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[[Category: Thomazeau, K.]]
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[[Category: allostery]]
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[[Category: plp enzyme]]
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[[Category: s-adenosyl-methionine]]
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[[Category: threonine biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:47:31 2007''
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Current revision

Structure of threonine synthase from Arabidopsis thaliana

PDB ID 1e5x

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