3vw5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<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 [https://en.wikipedia.org/wiki/ | <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=' | </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='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'>[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> | ||
</table> | </table> | ||
== Function == | == 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 == | ||
| Line 23: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fujiwara | [[Category: Ruminococcus albus]] | ||
[[Category: Saburi | [[Category: Fujiwara T]] | ||
[[Category: Tanaka | [[Category: Saburi W]] | ||
[[Category: Yao | [[Category: Tanaka I]] | ||
[[Category: Yao M]] | |||
Latest revision as of 15:39, 8 November 2023
Crystal structure of sugar epimerase from ruminal bacteriumCrystal structure of sugar epimerase from ruminal bacterium
Structural highlights
FunctionCEEP_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 PubMedEnzymatic 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
|
| ||||||||||||||||