7wrt: Difference between revisions
New page: '''Unreleased structure''' The entry 7wrt is ON HOLD Authors: Kamitori, S., Yoshihara, A. Description: X-ray structure ofThermus thermophilus HB8 transketorase demonstrate in complex w... |
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==X-ray structure ofThermus thermophilus HB8 transketorase demonstrate in complex with TPP and D-erythrose-4-phosphate== | |||
<StructureSection load='7wrt' size='340' side='right'caption='[[7wrt]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7wrt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WRT 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]] 2.25Å</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=E4P:ERYTHOSE-4-PHOSPHATE'>E4P</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=7wrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wrt OCA], [https://pdbe.org/7wrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wrt RCSB], [https://www.ebi.ac.uk/pdbsum/7wrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wrt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SM35_THET8 Q5SM35_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transketolase is a key enzyme in the pentose phosphate pathway in all organisms, recognizing sugar phosphates as substrates. Transketolase with a cofactor of thiamine pyrophosphate catalyzes the transfer of a 2-carbon unit from D-xylulose-5-phosphate to D-ribose-5-phosphate (5-carbon aldose), giving D-sedoheptulose-7-phosphate (7-carbon ketose). Transketolases can also recognize non-phosphorylated monosaccharides as substrates, and catalyze the formation of non-phosphorylated 7-carbon ketose (heptulose), which has attracted pharmaceutical attention as an inhibitor of sugar metabolism. Here, we report the structural and biochemical characterizations of transketolase from Thermus thermophilus HB8 (TtTK), a well-characterized thermophilic Gram-negative bacterium. TtTK showed marked thermostability with maximum enzyme activity at 85 degrees C, and efficiently catalyzed the formation of heptuloses from lithium hydroxypyruvate and four aldopentoses: D-ribose, L-lyxose, L-arabinose, and D-xylose. The X-ray structure showed that TtTK tightly forms a homodimer with more interactions between subunits compared with transketolase from other organisms, contributing to its thermal stability. A modeling study based on X-ray structures suggested that D-ribose and L-lyxose could bind to the catalytic site of TtTK to form favorable hydrogen bonds with the enzyme, explaining the high conversion rates of 41% (D-ribose) and 43% (L-lyxose) to heptulose. These results demonstrate the potential of TtTK as an enzyme producing a rare sugar of heptulose. KEY POINTS: * Transketolase catalyzes the formation of a 7-carbon sugar phosphate * Structural and biochemical characterizations of thermophilic transketolase were done * The enzyme could produce non-phosphorylated 7-carbon ketoses from sugars. | |||
Structural and biochemical characterizations of Thermus thermophilus HB8 transketolase producing a heptulose.,Yoshihara A, Takamatsu Y, Mochizuki S, Yoshida H, Masui R, Izumori K, Kamitori S Appl Microbiol Biotechnol. 2022 Nov 28. doi: 10.1007/s00253-022-12297-z. PMID:36441206<ref>PMID:36441206</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7wrt" style="background-color:#fffaf0;"></div> | ||
[[Category: Kamitori | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Kamitori S]] | |||
[[Category: Yoshihara A]] | |||
Latest revision as of 20:44, 29 November 2023
X-ray structure ofThermus thermophilus HB8 transketorase demonstrate in complex with TPP and D-erythrose-4-phosphateX-ray structure ofThermus thermophilus HB8 transketorase demonstrate in complex with TPP and D-erythrose-4-phosphate
Structural highlights
FunctionPublication Abstract from PubMedTransketolase is a key enzyme in the pentose phosphate pathway in all organisms, recognizing sugar phosphates as substrates. Transketolase with a cofactor of thiamine pyrophosphate catalyzes the transfer of a 2-carbon unit from D-xylulose-5-phosphate to D-ribose-5-phosphate (5-carbon aldose), giving D-sedoheptulose-7-phosphate (7-carbon ketose). Transketolases can also recognize non-phosphorylated monosaccharides as substrates, and catalyze the formation of non-phosphorylated 7-carbon ketose (heptulose), which has attracted pharmaceutical attention as an inhibitor of sugar metabolism. Here, we report the structural and biochemical characterizations of transketolase from Thermus thermophilus HB8 (TtTK), a well-characterized thermophilic Gram-negative bacterium. TtTK showed marked thermostability with maximum enzyme activity at 85 degrees C, and efficiently catalyzed the formation of heptuloses from lithium hydroxypyruvate and four aldopentoses: D-ribose, L-lyxose, L-arabinose, and D-xylose. The X-ray structure showed that TtTK tightly forms a homodimer with more interactions between subunits compared with transketolase from other organisms, contributing to its thermal stability. A modeling study based on X-ray structures suggested that D-ribose and L-lyxose could bind to the catalytic site of TtTK to form favorable hydrogen bonds with the enzyme, explaining the high conversion rates of 41% (D-ribose) and 43% (L-lyxose) to heptulose. These results demonstrate the potential of TtTK as an enzyme producing a rare sugar of heptulose. KEY POINTS: * Transketolase catalyzes the formation of a 7-carbon sugar phosphate * Structural and biochemical characterizations of thermophilic transketolase were done * The enzyme could produce non-phosphorylated 7-carbon ketoses from sugars. Structural and biochemical characterizations of Thermus thermophilus HB8 transketolase producing a heptulose.,Yoshihara A, Takamatsu Y, Mochizuki S, Yoshida H, Masui R, Izumori K, Kamitori S Appl Microbiol Biotechnol. 2022 Nov 28. doi: 10.1007/s00253-022-12297-z. PMID:36441206[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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