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1kl7

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[[Image:1kl7.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Threonine Synthase from Yeast==
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|PDB= 1kl7 |SIZE=350|CAPTION= <scene name='initialview01'>1kl7</scene>, resolution 2.7&Aring;
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<StructureSection load='1kl7' size='340' side='right'caption='[[1kl7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
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<table><tr><td colspan='2'>[[1kl7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KL7 FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.7&#8491;</td></tr>
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|GENE=
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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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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}}
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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=1kl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kl7 OCA], [https://pdbe.org/1kl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kl7 ProSAT]</span></td></tr>
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</table>
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'''Crystal Structure of Threonine Synthase from Yeast'''
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== Function ==
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[https://www.uniprot.org/uniprot/THRC_YEAST THRC_YEAST] Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine (By similarity).
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Threonine synthase catalyzes the final step of threonine biosynthesis, the pyridoxal 5'-phosphate (PLP)-dependent conversion of O-phosphohomoserine into threonine and inorganic phosphate. Threonine is an essential nutrient for mammals, and its biosynthetic machinery is restricted to bacteria, plants, and fungi; therefore, threonine synthase represents an interesting pharmaceutical target. The crystal structure of threonine synthase from Saccharomyces cerevisiae has been solved at 2.7 A resolution using multiwavelength anomalous diffraction. The structure reveals a monomer as active unit, which is subdivided into three distinct domains: a small N-terminal domain, a PLP-binding domain that covalently anchors the cofactor and a so-called large domain, which contains the main of the protein body. All three domains show the typical open alpha/beta architecture. The cofactor is bound at the interface of all three domains, buried deeply within a wide canyon that penetrates the whole molecule. Based on structural alignments with related enzymes, an enzyme-substrate complex was modeled into the active site of yeast threonine synthase, which revealed essentials for substrate binding and catalysis. Furthermore, the comparison with related enzymes of the beta-family of PLP-dependent enzymes indicated structural determinants of the oligomeric state and thus rationalized for the first time how a PLP enzyme acts in monomeric form.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/1kl7_consurf.spt"</scriptWhenChecked>
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1KL7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KL7 OCA].
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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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==Reference==
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</jmolCheckbox>
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Structure and function of threonine synthase from yeast., Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic' S, Huber R, Laber B, Bourenkov GP, Clausen T, J Biol Chem. 2002 Apr 5;277(14):12396-405. Epub 2001 Dec 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11756443 11756443]
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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=1kl7 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Bourenkov GP]]
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[[Category: Threonine synthase]]
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[[Category: Clausen T]]
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[[Category: Bourenkov, G P.]]
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[[Category: Ehlert S]]
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[[Category: Clausen, T.]]
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[[Category: Garrido-Franco M]]
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[[Category: Ehlert, S.]]
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[[Category: Huber R]]
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[[Category: Garrido-Franco, M.]]
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[[Category: Laber B]]
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[[Category: Huber, R.]]
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[[Category: Marinkovic S]]
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[[Category: Laber, B.]]
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[[Category: Messerschmidt A]]
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[[Category: Marinkovic, S.]]
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[[Category: Messerschmidt, A.]]
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[[Category: PLP]]
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[[Category: beta-family]]
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[[Category: monomer]]
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[[Category: pyridoxal 5-phosphate]]
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[[Category: threonine synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:18:56 2008''
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Current revision

Crystal Structure of Threonine Synthase from Yeast

PDB ID 1kl7

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