8cip
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of transketolase from Geobacillus stearothermophilus== | |
| - | + | <StructureSection load='8cip' size='340' side='right'caption='[[8cip]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8cip]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CIP FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8cip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cip OCA], [https://pdbe.org/8cip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cip RCSB], [https://www.ebi.ac.uk/pdbsum/8cip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cip ProSAT]</span></td></tr> |
| - | [[Category: Leogrande | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/TKT_GEOSE TKT_GEOSE] Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, likely via a covalent intermediate with the cofactor thiamine pyrophosphate. Can use L-erythrulose as donor and D-ribose-5-phosphate as acceptor substrates, forming glycolaldehyde and D-sedoheptulose-7-phosphate. For synthetic purposes, is able to use hydroxypyruvate (HPA) as donor substrate, making the reaction irreversible due to the release of carbon dioxide, and various aldehydes as acceptor substrates, which leads to the corresponding ketoses. Thus, using hydroxypyruvate as donor and three different aldehydes as acceptors, i.e. glycolaldehyde, D-glyceraldehyde and butyraldehyde, the enzyme stereoselectively forms the corresponding products L-erythrulose, D-xylulose and (3S)-1,3-dihydroxyhexan-2-one, respectively.[REFERENCE:2] |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Geobacillus stearothermophilus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Leogrande C]] | ||
| + | [[Category: Rabe von Pappenheim F]] | ||
| + | [[Category: Tittmann K]] | ||
Revision as of 06:03, 2 March 2023
Crystal structure of transketolase from Geobacillus stearothermophilus
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