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==Crystal structure of the mutant E494Q of GH92 alpha-1,2-mannosidase from Enterococcus faecalis ATCC 10100 in complex with alpha-1,2-mannobiose== | ==Crystal structure of the mutant E494Q of GH92 alpha-1,2-mannosidase from Enterococcus faecalis ATCC 10100 in complex with alpha-1,2-mannobiose== | ||
<StructureSection load='7fe2' size='340' side='right'caption='[[7fe2]]' scene=''> | <StructureSection load='7fe2' size='340' side='right'caption='[[7fe2]], [[Resolution|resolution]] 1.75Å' 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=7FE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FE2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7fe2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FE2 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=7fe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fe2 OCA], [https://pdbe.org/7fe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fe2 RCSB], [https://www.ebi.ac.uk/pdbsum/7fe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fe2 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=7fe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fe2 OCA], [https://pdbe.org/7fe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fe2 RCSB], [https://www.ebi.ac.uk/pdbsum/7fe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fe2 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The conformational changes in a sugar moiety along the hydrolytic pathway are key to understand the mechanism of glycoside hydrolases (GHs) and to design new inhibitors. The two predominant itineraries for mannosidases go via OS2 --> B2,5 --> 1S5 and 3S1 --> 3H4 --> 1C4. For the CAZy family 92, the conformational itinerary was unknown. Published complexes of Bacteroides thetaiotaomicron GH92 catalyst with a S-glycoside and mannoimidazole indicate a 4C1 --> 4H5/1S5 --> 1S5 mechanism. However, as observed with the GH125 family, S-glycosides may not act always as good mimics of GH's natural substrate. Here we present a cooperative study between computations and experiments where our results predict the E5 --> B2,5/1S5 --> 1S5 pathway for GH92 enzymes. Furthermore, we demonstrate the Michaelis complex mimicry of a new kind of C-disaccharides, whose biochemical applicability was still a chimera. | |||
Unlocking the hydrolytic mechanism of GH92 alpha-1,2-mannosidases: computation inspires using C-glycosides as Michaelis complex mimics.,Alonso-Gil S, Parkan K, Kaminsky J, Pohl R, Miyazaki T Chemistry. 2022 Jan 20. doi: 10.1002/chem.202200148. PMID:35049087<ref>PMID:35049087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7fe2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alonso-Gil S]] | [[Category: Alonso-Gil, S]] | ||
[[Category: Miyazaki T]] | [[Category: Miyazaki, T]] | ||
[[Category: Carbohydrate]] | |||
[[Category: Gh92]] | |||
[[Category: Glycoside hydrolase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Inhibitor]] | |||
[[Category: N-glycan]] | |||
Revision as of 14:00, 16 February 2022
Crystal structure of the mutant E494Q of GH92 alpha-1,2-mannosidase from Enterococcus faecalis ATCC 10100 in complex with alpha-1,2-mannobioseCrystal structure of the mutant E494Q of GH92 alpha-1,2-mannosidase from Enterococcus faecalis ATCC 10100 in complex with alpha-1,2-mannobiose
Structural highlights
Publication Abstract from PubMedThe conformational changes in a sugar moiety along the hydrolytic pathway are key to understand the mechanism of glycoside hydrolases (GHs) and to design new inhibitors. The two predominant itineraries for mannosidases go via OS2 --> B2,5 --> 1S5 and 3S1 --> 3H4 --> 1C4. For the CAZy family 92, the conformational itinerary was unknown. Published complexes of Bacteroides thetaiotaomicron GH92 catalyst with a S-glycoside and mannoimidazole indicate a 4C1 --> 4H5/1S5 --> 1S5 mechanism. However, as observed with the GH125 family, S-glycosides may not act always as good mimics of GH's natural substrate. Here we present a cooperative study between computations and experiments where our results predict the E5 --> B2,5/1S5 --> 1S5 pathway for GH92 enzymes. Furthermore, we demonstrate the Michaelis complex mimicry of a new kind of C-disaccharides, whose biochemical applicability was still a chimera. Unlocking the hydrolytic mechanism of GH92 alpha-1,2-mannosidases: computation inspires using C-glycosides as Michaelis complex mimics.,Alonso-Gil S, Parkan K, Kaminsky J, Pohl R, Miyazaki T Chemistry. 2022 Jan 20. doi: 10.1002/chem.202200148. PMID:35049087[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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