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

spinqualitylabelsall models 4wsj, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wsj is a 4 chain structure with sequence from Bacteroides thetaiotaomicron VPI-5482. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.64Å Ligands: 3U3, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8A3I4_BACTN Publication Abstract from PubMed GH29 alpha-l-fucosidases catalyze the hydrolysis of alpha-l-fucosidic linkages. Deficiency in human lysosomal alpha-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 in vitro and in vivo labeling of GH29 alpha-l-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial alpha-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 alpha-l-fucosidase inhibitor from eight configurational isomers. In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 alpha-l-fucosidases.,Jiang J, Kallemeijn WW, Wright DW, van den Nieuwendijk AMCH, Rohde VC, Folch EC, van den Elst H, Florea BI, Scheij S, Donker-Koopman WE, Verhoek M, Li N, Schurmann M, Mink D, Boot RG, Codee JDC, van der Marel GA, Davies GJ, Aerts JMFG, Overkleeft HS Chem Sci. 2015 May 1;6(5):2782-false. doi: 10.1039/c4sc03739a. Epub 2015 Feb 9. PMID:29142681 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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