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6rqk
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole== | |
| + | <StructureSection load='6rqk' size='340' side='right'caption='[[6rqk]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rqk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_str._13 Clostridium perfringens str. 13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RQK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MVL:(5R,6R,7S,8R)-5-(HYDROXYMETHYL)-5,6,7,8-TETRAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL'>MVL</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=6rqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rqk OCA], [https://pdbe.org/6rqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rqk RCSB], [https://www.ebi.ac.uk/pdbsum/6rqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rqk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8XNB2_CLOPE Q8XNB2_CLOPE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannosides, is shown to bind in a B2,5 conformation on the Clostridium perfringens GH125 alpha-1,6-mannosidase, providing additional evidence of a OS2-B2,5-1S5 conformational itinerary for enzymes of this family. | ||
| - | + | Distortion of mannoimidazole supports a B2,5 boat transition state for the family GH125 alpha-1,6-mannosidase from Clostridium perfringens.,Males A, Speciale G, Williams SJ, Davies GJ Org Biomol Chem. 2019 Aug 13. doi: 10.1039/c9ob01161g. PMID:31407758<ref>PMID:31407758</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6rqk" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Mannosidase 3D structures|Mannosidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Clostridium perfringens str. 13]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Davies GJ]] | ||
| + | [[Category: Males A]] | ||
Current revision
Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole
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