4WSJ
Crystal structure of a bacterial fucodiase in complex with 1-((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)ethan-1-one
Summary for 4WSJ
| Entry DOI | 10.2210/pdb4wsj/pdb |
| Descriptor | Alpha-L-fucosidase, SULFATE ION, N-[(1S,2R,3R,4S,5R)-3,4,5-trihydroxy-2-methylcyclohexyl]acetamide, ... (4 entities in total) |
| Functional Keywords | fucosidase complex covalent inhibitor, hydrolase |
| Biological source | Bacteroides thetaiotaomicron |
| Total number of polymer chains | 4 |
| Total formula weight | 207386.49 |
| Authors | Davies, G.J.,Wright, D.W. (deposition date: 2014-10-28, release date: 2014-11-05, Last modification date: 2024-10-23) |
| Primary citation | Jiang, J.,Kallemeijn, W.W.,Wright, D.W.,van den Nieuwendijk, A.M.C.H.,Rohde, V.C.,Folch, E.C.,van den Elst, H.,Florea, B.I.,Scheij, S.,Donker-Koopman, W.E.,Verhoek, M.,Li, N.,Schurmann, M.,Mink, D.,Boot, R.G.,Codee, J.D.C.,van der Marel, G.A.,Davies, G.J.,Aerts, J.M.F.G.,Overkleeft, H.S. In vitroandin vivocomparative and competitive activity-based protein profiling of GH29 alpha-l-fucosidases. Chem Sci, 6:2782-false, 2015 Cited by PubMed Abstract: GH29 α-l-fucosidases catalyze the hydrolysis of α-l-fucosidic linkages. Deficiency in human lysosomal α-l-fucosidase (FUCA1) leads to the recessively inherited disorder, fucosidosis. Herein we describe the development of fucopyranose-configured cyclophellitol aziridines as activity-based probes (ABPs) for selective and labeling of GH29 α-l-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial α-l-fucosidase confirms that the ABPs act by covalent modification of the active site nucleophile. Competitive activity-based protein profiling identified l-fuconojirimycin as the single GH29 α-l-fucosidase inhibitor from eight configurational isomers. PubMed: 29142681DOI: 10.1039/c4sc03739a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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