5xqa
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Transketolase in complex with ribose-5-phosphate from Pichia Stipitis== | |
| + | <StructureSection load='5xqa' size='340' side='right'caption='[[5xqa]], [[Resolution|resolution]] 1.14Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xqa]] 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=5XQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XQA FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HSX:5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE'>HSX</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></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=5xqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqa OCA], [https://pdbe.org/5xqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xqa RCSB], [https://www.ebi.ac.uk/pdbsum/5xqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqa ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5xqa" style="background-color:#fffaf0;"></div> |
| - | [[Category: Hsu | + | |
| - | [[Category: Wang | + | ==See Also== |
| + | *[[Transketolase 3D structures|Transketolase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Scheffersomyces stipitis CBS 6054]] | ||
| + | [[Category: Hsu NS]] | ||
| + | [[Category: Li TL]] | ||
| + | [[Category: Wang YL]] | ||
Current revision
Crystal Structure of Transketolase in complex with ribose-5-phosphate from Pichia Stipitis
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