5xqa

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<StructureSection load='5xqa' size='340' side='right' caption='[[5xqa]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
<StructureSection load='5xqa' size='340' side='right' caption='[[5xqa]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xqa]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XQA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xqa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Picst Picst]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XQA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TKT, TKT1, PICST_67105 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322104 PICST])</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='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='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=5xqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqa OCA], [http://pdbe.org/5xqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xqa RCSB], [http://www.ebi.ac.uk/pdbsum/5xqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqa 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=5xqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xqa OCA], [http://pdbe.org/5xqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xqa RCSB], [http://www.ebi.ac.uk/pdbsum/5xqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xqa ProSAT]</span></td></tr>
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== Function ==
== 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.
[[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5xqa" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Transketolase|Transketolase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Picst]]
[[Category: Transketolase]]
[[Category: Transketolase]]
[[Category: Hsu, N S]]
[[Category: Hsu, N S]]

Revision as of 08:44, 19 December 2018

Crystal Structure of Transketolase in complex with ribose-5-phosphate from Pichia Stipitis

5xqa, resolution 1.14Å

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