4v27: Difference between revisions
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''' | ==Structure of the GH99 endo-alpha-mannanase from Bacteroides xylanisolvens in complex with mannose-alpha-1,3-isofagomine== | ||
<StructureSection load='4v27' size='340' side='right' caption='[[4v27]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4v27]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V27 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IFM:5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE'>IFM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v1r|4v1r]], [[4v1s|4v1s]], [[4v28|4v28]]</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=4v27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v27 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v27 RCSB], [http://www.ebi.ac.uk/pdbsum/4v27 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:25487964</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glycoprotein endo-alpha-1,2-mannosidase]] | |||
[[Category: Bellmaine, S]] | |||
[[Category: Davies, G J]] | |||
[[Category: Hakki, Z]] | |||
[[Category: Speciale, G]] | |||
[[Category: Thompson, A J]] | |||
[[Category: Williams, S J]] | |||
[[Category: Bacteroide]] | |||
[[Category: Cazy]] | |||
[[Category: Enzyme-carbohydrate interaction]] | |||
[[Category: Gh99]] | |||
[[Category: Glycosidase inhibition]] | |||
[[Category: Hydrolase]] | |||
[[Category: Inhibitor]] | |||
[[Category: Mannan]] | |||
[[Category: Polysaccharide utilisation]] | |||
Revision as of 11:01, 24 December 2014
Structure of the GH99 endo-alpha-mannanase from Bacteroides xylanisolvens in complex with mannose-alpha-1,3-isofagomine
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