6yak: Difference between revisions

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==Split gene transketolase, active alpha2beta2 heterotetramer==
<StructureSection load='6yak' size='340' side='right'caption='[[6yak]]' scene=''>
<StructureSection load='6yak' size='340' side='right'caption='[[6yak]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
<table><tr><td colspan='2'>[[6yak]] 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=6YAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YAK FirstGlance]. <br>
</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=6yak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yak OCA], [http://pdbe.org/6yak PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yak RCSB], [http://www.ebi.ac.uk/pdbsum/6yak PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yak ProSAT]</span></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]] 1.34&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8EL:2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-2H-1,3-thiazol-5-yl]ethyl+phosphono+hydrogen+phosphate'>8EL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</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=6yak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yak OCA], [https://pdbe.org/6yak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yak RCSB], [https://www.ebi.ac.uk/pdbsum/6yak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yak ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yak" style="background-color:#fffaf0;"></div>
==See Also==
*[[Transketolase 3D structures|Transketolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Carboxydothermus hydrogenoformans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Z-disk]]
[[Category: Isupov MN]]
[[Category: James P]]
[[Category: Littlechild JA]]

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