3vni: Difference between revisions
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<StructureSection load='3vni' size='340' side='right'caption='[[3vni]], [[Resolution|resolution]] 1.98Å' scene=''> | <StructureSection load='3vni' size='340' side='right'caption='[[3vni]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vni]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3vni]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum_H10 Ruminiclostridium cellulolyticum H10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VNI FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=3vni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vni OCA], [https://pdbe.org/3vni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vni RCSB], [https://www.ebi.ac.uk/pdbsum/3vni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vni ProSAT]</span></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=3vni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vni OCA], [https://pdbe.org/3vni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vni RCSB], [https://www.ebi.ac.uk/pdbsum/3vni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vni ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DPES_RUMCH DPES_RUMCH] Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose.<ref>PMID:21663329</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chan | [[Category: Ruminiclostridium cellulolyticum H10]] | ||
[[Category: Chen | [[Category: Chan HC]] | ||
[[Category: Guo | [[Category: Chen CC]] | ||
[[Category: Hu | [[Category: Guo RT]] | ||
[[Category: Huang | [[Category: Hu Y]] | ||
[[Category: Ko | [[Category: Huang CH]] | ||
[[Category: Ren | [[Category: Ko TP]] | ||
[[Category: Sun | [[Category: Ren F]] | ||
[[Category: Zhu | [[Category: Sun Y]] | ||
[[Category: Zhu Y]] | |||
Latest revision as of 15:28, 8 November 2023
Crystal structures of D-Psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugarsCrystal structures of D-Psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars
Structural highlights
FunctionDPES_RUMCH Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose.[1] Publication Abstract from PubMedD-psicose 3-epimerase (DPEase) is demonstrated to be useful in the bioproduction of D-psicose, a rare hexose sugar, from D-fructose, found plenty in nature. Clostridium cellulolyticum H10 has recently been identified as a DPEase that can epimerize D-fructose to yield D-psicose with a much higher conversion rate when compared with the conventionally used DTEase. In this study, the crystal structure of the C. cellulolyticum DPEase was determined. The enzyme assembles into a tetramer and each subunit shows a (beta/alpha)(8) TIM barrel fold with a Mn(2+) metal ion in the active site. Additional crystal structures of the enzyme in complex with substrates/products (D-psicose, D-fructose, D-tagatose and D-sorbose) were also determined. From the complex structures of C. cellulolyticum DPEase with D-psicose and D-fructose, the enzyme has much more interactions with D-psicose than D-fructose by forming more hydrogen bonds between the substrate and the active site residues. Accordingly, based on these ketohexose-bound complex structures, a C3-O3 proton-exchange mechanism for the conversion between D-psicose and D-fructose is proposed here. These results provide a clear idea for the deprotonation/protonation roles of E150 and E244 in catalysis. Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars.,Chan HC, Zhu Y, Hu Y, Ko TP, Huang CH, Ren F, Chen CC, Ma Y, Guo RT, Sun Y Protein Cell. 2012 Feb;3(2):123-31. Epub 2012 Mar 17. PMID:22426981[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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