5xtx: Difference between revisions

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 ==Crystal Structure of Transketolase in complex with TPP intermediate VII from Pichia Stipitis==
-<StructureSection load='5xtx' size='340' side='right' caption='[[5xtx]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
+<StructureSection load='5xtx' size='340' side='right'caption='[[5xtx]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xtx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XTX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xtx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scheffersomyces_stipitis_CBS_6054 Scheffersomyces stipitis CBS 6054]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XTX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8ML:2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methylidene-2-[(2S,3S,4R,5R)-1,2,3,4,5-pentakis(oxidanyl)-6-phosphonooxy-hexan-2-yl]-1,3-thiazolidin-5-yl]ethyl+phosphono+hydrogen+phosphate'>8ML</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.049&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transketolase Transketolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8ML:2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methylidene-2-[(2S,3S,4R,5R)-1,2,3,4,5-pentakis(oxidanyl)-6-phosphonooxy-hexan-2-yl]-1,3-thiazolidin-5-yl]ethyl+phosphono+hydrogen+phosphate'>8ML</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=5xtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtx OCA], [http://pdbe.org/5xtx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xtx RCSB], [http://www.ebi.ac.uk/pdbsum/5xtx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtx ProSAT]</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=5xtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xtx OCA], [https://pdbe.org/5xtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xtx RCSB], [https://www.ebi.ac.uk/pdbsum/5xtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xtx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TKT_PICST TKT_PICST]] Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
+[https://www.uniprot.org/uniprot/TKT_PICST TKT_PICST] Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Transketolase (TK) catalyzes a reversible transfer of a two-carbon (C2 ) unit between phosphoketose donors and phosphoaldose acceptors, for which the group-transfer reaction that follows a one- or two-electron mechanism and the force that breaks the C2"-C3" bond of the ketose donors remain unresolved. Herein, we report ultrahigh-resolution crystal structures of a TK (TKps) from Pichia stipitis in previously undiscovered intermediate states and support a diradical mechanism for a reversible group-transfer reaction. In conjunction with MS, NMR spectroscopy, EPR and computational analyses, it is concluded that the enzyme-catalyzed non-Kekule diradical cofactor brings about the C2"-C3" bond cleavage/formation for the C2 -unit transfer reaction, for which suppression of activation energy and activation and destabilization of enzymatic intermediates are facilitated.
+Evidence of Diradicals Involved in the Yeast Transketolase Catalyzed Keto-Transferring Reactions.,Hsu NS, Wang YL, Lin KH, Chang CF, Ke SC, Lyu SY, Hsu LJ, Li YS, Chen SC, Wang KC, Li TL Chembiochem. 2018 Nov 16;19(22):2395-2402. doi: 10.1002/cbic.201800378. Epub 2018, Oct 18. PMID:30155962<ref>PMID:30155962</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5xtx" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transketolase 3D structures|Transketolase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Transketolase]]
+[[Category: Large Structures]]
-[[Category: Hsu, N S]]
+[[Category: Scheffersomyces stipitis CBS 6054]]
-[[Category: Li, T L]]
+[[Category: Hsu NS]]
-[[Category: Wang, Y L]]
+[[Category: Li TL]]
-[[Category: Transferase]]
+[[Category: Wang YL]]