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| | <StructureSection load='4v28' size='340' side='right'caption='[[4v28]], [[Resolution|resolution]] 1.20Å' scene=''> | | <StructureSection load='4v28' size='340' side='right'caption='[[4v28]], [[Resolution|resolution]] 1.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v28]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteroides_sp._xb1a Bacteroides sp. xb1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V28 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v28]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_xylanisolvens_XB1A Bacteroides xylanisolvens XB1A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V28 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MU:7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE'>4MU</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4MU:7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE'>4MU</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PRD_900112:3alpha-alpha-mannobiose'>PRD_900112</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v1r|4v1r]], [[4v1s|4v1s]], [[4v27|4v27]]</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=4v28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v28 OCA], [https://pdbe.org/4v28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v28 RCSB], [https://www.ebi.ac.uk/pdbsum/4v28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v28 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycoprotein_endo-alpha-1,2-mannosidase Glycoprotein endo-alpha-1,2-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.130 3.2.1.130] </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=4v28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v28 OCA], [http://pdbe.org/4v28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v28 RCSB], [http://www.ebi.ac.uk/pdbsum/4v28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v28 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D6D1V7_9BACE D6D1V7_9BACE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteroides sp. xb1a]] | + | [[Category: Bacteroides xylanisolvens XB1A]] |
| - | [[Category: Glycoprotein endo-alpha-1,2-mannosidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bellmaine, S]] | + | [[Category: Bellmaine S]] |
| - | [[Category: Davies, G J]] | + | [[Category: Davies GJ]] |
| - | [[Category: Hakki, Z]] | + | [[Category: Hakki Z]] |
| - | [[Category: Speciale, G]] | + | [[Category: Speciale G]] |
| - | [[Category: Thompson, A J]] | + | [[Category: Thompson AJ]] |
| - | [[Category: Williams, S J]] | + | [[Category: Williams SJ]] |
| - | [[Category: Bacteroide]]
| + | |
| - | [[Category: Cazy]]
| + | |
| - | [[Category: Enzyme-carbohydrate interaction]]
| + | |
| - | [[Category: Gh99]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mannan]]
| + | |
| - | [[Category: Polysaccharide utilisation]]
| + | |
| - | [[Category: Substrate complex]]
| + | |
| Structural highlights
Function
D6D1V7_9BACE
Publication Abstract from PubMed
Glycoside hydrolase family 99 (GH99) was created to categorize sequence-related glycosidases possessing endo-alpha-mannosidase activity: the cleavage of mannosidic linkages within eukaryotic N-glycan precursors (Glc1-3 Man9 GlcNAc2 ), releasing mono-, di- and triglucosylated-mannose (Glc1-3 -1,3-Man). GH99 family members have recently been implicated in the ability of Bacteroides spp., present within the gut microbiota, to metabolize fungal cell wall alpha-mannans, releasing alpha-1,3-mannobiose by hydrolysing alphaMan-1,3-alphaMan-->1,2-alphaMan-1,2-alphaMan sequences within branches off the main alpha-1,6-mannan backbone. We report the development of a series of substrates and inhibitors, which we use to kinetically and structurally characterise this novel endo-alpha-1,2-mannanase activity of bacterial GH99 enzymes from Bacteroides thetaiotaomicron and xylanisolvens. These data reveal an approximate 5 kJ mol-1 preference for mannose-configured substrates in the -2 subsite (relative to glucose), which inspired the development of a new inhibitor, alpha-mannopyranosyl-1,3-isofagomine (ManIFG), the most potent (bacterial) GH99 inhibitor reported to date. X-ray structures of ManIFG or a substrate in complex with wild-type or inactive mutants, respectively, of B. xylanisolvens GH99 reveal the structural basis for binding to D-mannose- rather than D-glucose-configured substrates.
Structural and Kinetic Dissection of the endo-alpha-1,2-Mannanase Activity of Bacterial GH99 Glycoside Hydrolases from Bacteroides spp.,Hakki Z, Thompson AJ, Bellmaine S, Speciale G, Davies GJ, Williams SJ Chemistry. 2014 Dec 8. doi: 10.1002/chem.201405539. PMID:25487964[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hakki Z, Thompson AJ, Bellmaine S, Speciale G, Davies GJ, Williams SJ. Structural and Kinetic Dissection of the endo-alpha-1,2-Mannanase Activity of Bacterial GH99 Glycoside Hydrolases from Bacteroides spp. Chemistry. 2014 Dec 8. doi: 10.1002/chem.201405539. PMID:25487964 doi:http://dx.doi.org/10.1002/chem.201405539
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