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| | ==Crystal structure of sugar epimerase from ruminal bacterium== | | ==Crystal structure of sugar epimerase from ruminal bacterium== |
| - | <StructureSection load='3vw5' size='340' side='right' caption='[[3vw5]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3vw5' size='340' side='right'caption='[[3vw5]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vw5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ruminococcus_albus Ruminococcus albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VW5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vw5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminococcus_albus Ruminococcus albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VW5 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1264 Ruminococcus albus])</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]] 2.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellobiose_epimerase Cellobiose epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.11 5.1.3.11] </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=3vw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vw5 OCA], [https://pdbe.org/3vw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vw5 RCSB], [https://www.ebi.ac.uk/pdbsum/3vw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vw5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vw5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vw5 RCSB], [http://www.ebi.ac.uk/pdbsum/3vw5 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CEEP_RUMAL CEEP_RUMAL] Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also epimerize cellotriose to Glc-Glc-Man, cellotetraose to Glc-Glc-Glc-Man, and lactose to epilactose.[HAMAP-Rule:MF_00929]<ref>PMID:17612504</ref> <ref>PMID:18392616</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3vw5" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cellobiose epimerase]] | + | [[Category: Large Structures]] |
| | [[Category: Ruminococcus albus]] | | [[Category: Ruminococcus albus]] |
| - | [[Category: Fujiwara, T]] | + | [[Category: Fujiwara T]] |
| - | [[Category: Saburi, W]] | + | [[Category: Saburi W]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Tanaka I]] |
| - | [[Category: Yao, M]] | + | [[Category: Yao M]] |
| - | [[Category: Carbohydrate/sugar binding]]
| + | |
| - | [[Category: Epimerase]]
| + | |
| - | [[Category: Epimerization]]
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| - | [[Category: Isomerase]]
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| Structural highlights
Function
CEEP_RUMAL Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). Can also epimerize cellotriose to Glc-Glc-Man, cellotetraose to Glc-Glc-Glc-Man, and lactose to epilactose.[HAMAP-Rule:MF_00929][1] [2]
Publication Abstract from PubMed
Enzymatic epimerization is an important modification for carbohydrates to acquire diverse functions attributable to their stereoisomers. Cellobiose 2-epimerase (CE) catalyzes interconversion between d-glucose and d-mannose residues at the reducing end of beta-1,4-linked oligosaccharides. Here, we solved the structure of Ruminococcus albus CE (RaCE). The structure of RaCE showed strong similarity to those of N-acetyl-D-glucosamine 2-epimerase and aldose-ketose isomerase YihS with a high degree of conservation of residues around the catalytic center, although sequence identity between them is low. Based on structural comparison, we found that His184 is required for RaCE activity as the third histidine added to two essential histidines in other sugar epimerases/isomerases. This finding was confirmed by mutagenesis, suggesting a new catalytic mechanism for CE involving three histidines.
Crystal structure of Ruminococcus albus cellobiose 2-epimerase: structural insights into epimerization of unmodified sugar.,Fujiwara T, Saburi W, Inoue S, Mori H, Matsui H, Tanaka I, Yao M FEBS Lett. 2013 Apr 2;587(7):840-6. doi: 10.1016/j.febslet.2013.02.007. Epub 2013, Feb 24. PMID:23462136[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ito S, Hamada S, Yamaguchi K, Umene S, Ito H, Matsui H, Ozawa T, Taguchi H, Watanabe J, Wasaki J, Ito S. Cloning and sequencing of the cellobiose 2-epimerase gene from an obligatory anaerobe, Ruminococcus albus. Biochem Biophys Res Commun. 2007 Aug 31;360(3):640-5. PMID:17612504 doi:10.1016/j.bbrc.2007.06.091
- ↑ Ito S, Taguchi H, Hamada S, Kawauchi S, Ito H, Senoura T, Watanabe J, Nishimukai M, Ito S, Matsui H. Enzymatic properties of cellobiose 2-epimerase from Ruminococcus albus and the synthesis of rare oligosaccharides by the enzyme. Appl Microbiol Biotechnol. 2008 Jun;79(3):433-41. PMID:18392616 doi:10.1007/s00253-008-1449-7
- ↑ Fujiwara T, Saburi W, Inoue S, Mori H, Matsui H, Tanaka I, Yao M. Crystal structure of Ruminococcus albus cellobiose 2-epimerase: structural insights into epimerization of unmodified sugar. FEBS Lett. 2013 Apr 2;587(7):840-6. doi: 10.1016/j.febslet.2013.02.007. Epub 2013, Feb 24. PMID:23462136 doi:10.1016/j.febslet.2013.02.007
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