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7cj7
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==Crystal structure of homo dimeric D-allulose 3-epimerase from Methylomonas sp. in complex with L-tagatose== | ==Crystal structure of homo dimeric D-allulose 3-epimerase from Methylomonas sp. in complex with L-tagatose== | ||
| - | <StructureSection load='7cj7' size='340' side='right'caption='[[7cj7]]' scene=''> | + | <StructureSection load='7cj7' size='340' side='right'caption='[[7cj7]], [[Resolution|resolution]] 1.69Å' 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=7CJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CJ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7cj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylomonas_sp._DH-1 Methylomonas sp. DH-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CJ7 FirstGlance]. <br> |
| - | </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=7cj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cj7 OCA], [https://pdbe.org/7cj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cj7 RCSB], [https://www.ebi.ac.uk/pdbsum/7cj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cj7 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]] 1.695Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FZU:(2R,3R,4R,5S)-2-(hydroxymethyl)oxane-2,3,4,5-tetrol'>FZU</scene>, <scene name='pdbligand=LTG:L-TAGATOSE'>LTG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SOL:L-SORBOSE'>SOL</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=7cj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cj7 OCA], [https://pdbe.org/7cj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cj7 RCSB], [https://www.ebi.ac.uk/pdbsum/7cj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cj7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A172U6X0_9GAMM A0A172U6X0_9GAMM] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | D-allulose has potential as a low calorie sweetener which can suppress fat accumulation. Several enzymes capable of D-allulose production have been isolated, including D-tagatose 3-epimerases. Here, we report the isolation of a novel protein from Methylomonas sp. expected to be a putative enzyme based on sequence similarity to ketose 3-epimerase. The synthesized gene encoding the deduced ketose 3-epimerase was expressed as a recombinant enzyme in E. coli, and it exhibited the highest enzymatic activity toward L-ribulose, followed by D-ribulose and D-allulose. The X-ray structure analysis of L-ribulose 3-epimerase from Methylomonas sp. (MetLRE) revealed a homodimeric enzyme, the first reported structure of dimeric L-ribulose 3-epimerase. The monomeric structure of MetLRE is similar to that of homotetrameric L-ribulose 3-epimerases, but the short C-terminal alpha-helix of MetLRE is unique and different from those of known L-ribulose 3 epimerases. The length of the C-terminal alpha-helix was thought to be involved in tetramerization and increasing stability; however, the addition of residues to MetLRE at the C-terminus did not lead to tetramer formation. MetLRE is the first dimeric L-ribulose 3-epimerase identified to exhibit high relative activity toward D-allulose. | ||
| + | |||
| + | Crystal structure of a novel homodimeric L-ribulose 3-epimerase from Methylomonus sp.,Yoshida H, Yoshihara A, Kato S, Mochizuki S, Akimitsu K, Izumori K, Kamitori S FEBS Open Bio. 2021 Apr 10. doi: 10.1002/2211-5463.13159. PMID:33838083<ref>PMID:33838083</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7cj7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Methylomonas sp. DH-1]] | ||
[[Category: Kamitori S]] | [[Category: Kamitori S]] | ||
[[Category: Yoshida H]] | [[Category: Yoshida H]] | ||
[[Category: Yoshihara A]] | [[Category: Yoshihara A]] | ||
Current revision
Crystal structure of homo dimeric D-allulose 3-epimerase from Methylomonas sp. in complex with L-tagatose
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