6yaj

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Current revision (13:22, 24 January 2024) (edit) (undo)
 
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==Split gene transketolase, inactive beta4 tetramer==
==Split gene transketolase, inactive beta4 tetramer==
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<StructureSection load='6yaj' size='340' side='right'caption='[[6yaj]]' scene=''>
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<StructureSection load='6yaj' size='340' side='right'caption='[[6yaj]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YAJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YAJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6yaj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YAJ FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yaj OCA], [http://pdbe.org/6yaj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yaj RCSB], [http://www.ebi.ac.uk/pdbsum/6yaj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yaj ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yaj OCA], [https://pdbe.org/6yaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yaj RCSB], [https://www.ebi.ac.uk/pdbsum/6yaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yaj ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A novel transketolase has been reconstituted from two separate polypeptide chains encoded by a 'split-gene' identified in the genome of the hyperthermophilic bacterium, Carboxydothermus hydrogenoformans. The reconstituted active alpha2beta2 tetrameric enzyme has been biochemically characterized and its activity has been determined using a range of aldehydes including glycolaldehyde, phenylacetaldehyde and cyclohexanecarboxaldehyde as the ketol acceptor and hydroxypyruvate as the donor. This reaction proceeds to near 100% completion due to the release of the product carbon dioxide and can be used for the synthesis of a range of sugars of interest to the pharmaceutical industry. This novel reconstituted transketolase is thermally stable with no loss of activity after incubation for 1 h at 70 degrees C and is stable after 1 h incubation with 50% of the organic solvents methanol, ethanol, isopropanol, DMSO, acetonitrile and acetone. The X-ray structure of the holo reconstituted alpha2beta2 tetrameric transketolase has been determined to 1.4 A resolution. In addition, the structure of an inactive tetrameric beta4 protein has been determined to 1.9 A resolution. The structure of the active reconstituted alpha2beta2 enzyme has been compared to the structures of related enzymes; the E1 component of the pyruvate dehydrogenase complex and D-xylulose-5-phosphate synthase, in an attempt to rationalize differences in structure and substrate specificity between these enzymes. This is the first example of a reconstituted 'split-gene' transketolase to be biochemically and structurally characterized allowing its potential for industrial biocatalysis to be evaluated.
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A 'Split-Gene' Transketolase From the Hyper-Thermophilic Bacterium Carboxydothermus hydrogenoformans: Structure and Biochemical Characterization.,James P, Isupov MN, De Rose SA, Sayer C, Cole IS, Littlechild JA Front Microbiol. 2020 Oct 30;11:592353. doi: 10.3389/fmicb.2020.592353., eCollection 2020. PMID:33193259<ref>PMID:33193259</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 6yaj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Transketolase 3D structures|Transketolase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Carboxydothermus hydrogenoformans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Isupov MN]]
[[Category: Isupov MN]]
[[Category: James P]]
[[Category: James P]]
[[Category: Littlechild JA]]
[[Category: Littlechild JA]]

Current revision

Split gene transketolase, inactive beta4 tetramer

PDB ID 6yaj

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