6rqk
From Proteopedia
(Difference between revisions)
m (Protected "6rqk" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RQK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rqk OCA], [http://pdbe.org/6rqk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rqk RCSB], [http://www.ebi.ac.uk/pdbsum/6rqk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rqk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Davies, G J]] | ||
| + | [[Category: Males, A]] | ||
| + | [[Category: Carbohydrate]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Glycoside hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Inhibitor]] | ||
Revision as of 15:42, 28 August 2019
Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole
| |||||||||||
