View source for 7cj8


==Crystal structure of N-terminal His-tagged D-allulose 3-epimerase from Methylomonas sp. in complex with D-allulose==
<StructureSection load='7cj8' size='340' side='right'caption='[[7cj8]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cj8]] is a 6 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=7CJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CJ8 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PSJ:D-PSICOSE'>PSJ</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=7cj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cj8 OCA], [https://pdbe.org/7cj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cj8 RCSB], [https://www.ebi.ac.uk/pdbsum/7cj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cj8 ProSAT]</span></td></tr>
</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cj8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylomonas sp. DH-1]]
[[Category: Kamitori S]]
[[Category: Yoshida H]]
[[Category: Yoshihara A]]