2x09

Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine- configured castanospermine and an amino-australine analogue

spinqualitylabelsall models 2x09, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x09 is a 2 chain structure with sequence from Amycolatopsis orientalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CD, X09 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EBDG_AMYOR Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The synthesis of amino-derivatives of castanospermine and australine and their characterisation as inhibitors of the exo-beta-D-glucosaminidase CsxA through enzyme kinetics and X-ray structural analysis is described. Inhibition of the exo-beta-D-glucosaminidase CsxA by a glucosamine-configured castanospermine and an amino-australine analogue.,Pluvinage B, Ghinet MG, Brzezinski R, Boraston AB, Stubbs KA Org Biomol Chem. 2009 Oct 21;7(20):4169-72. Epub 2009 Aug 14. PMID:19795054 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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