|
|
| (2 intermediate revisions not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1kl7' size='340' side='right'caption='[[1kl7]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1kl7' size='340' side='right'caption='[[1kl7]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kl7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KL7 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | <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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kl7 OCA], [http://pdbe.org/1kl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kl7 RCSB], [http://www.ebi.ac.uk/pdbsum/1kl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kl7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 16: |
Line 15: |
| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/1kl7_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/1kl7_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 34: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Threonine synthase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Bourenkov, G P]] | + | [[Category: Bourenkov GP]] |
| - | [[Category: Clausen, T]] | + | [[Category: Clausen T]] |
| - | [[Category: Ehlert, S]] | + | [[Category: Ehlert S]] |
| - | [[Category: Garrido-Franco, M]] | + | [[Category: Garrido-Franco M]] |
| - | [[Category: Huber, R]] | + | [[Category: Huber R]] |
| - | [[Category: Laber, B]] | + | [[Category: Laber B]] |
| - | [[Category: Marinkovic, S]] | + | [[Category: Marinkovic S]] |
| - | [[Category: Messerschmidt, A]] | + | [[Category: Messerschmidt A]] |
| - | [[Category: Beta-family]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Monomer]]
| + | |
| - | [[Category: Pyridoxal 5-phosphate]]
| + | |
| - | [[Category: Threonine synthesis]]
| + | |
| Structural highlights
Function
THRC_YEAST Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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:11756443[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic' S, Huber R, Laber B, Bourenkov GP, Clausen T. Structure and function of threonine synthase from yeast. J Biol Chem. 2002 Apr 5;277(14):12396-405. Epub 2001 Dec 26. PMID:11756443 doi:10.1074/jbc.M108734200
|
