4r27

Crystal structure of beta-glycosidase BGL167

spinqualitylabelsall models 4r27, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r27 is a 2 chain structure with sequence from Microbacterium sp. Gsoil167. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.03Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L0ELG0_9MICO Publication Abstract from PubMed Triterpenoids with desired glycosylation patterns have attracted considerable attention as potential therapeutics for inflammatory diseases and various types of cancer. Sugar-hydrolyzing enzymes with high substrate specificity would be far more efficient than other methods for the synthesis of such specialty triterpenoids, but they are yet to be developed. Here we present a strategy to rationally design a beta-glycosidase with high regiospecificity for triterpenoids. A beta-glycosidase with broad substrate specificity was isolated, and its crystal structure was determined at 2.0 A resolution. Based on the product profiles and substrate docking simulations, we modeled the substrate binding modes of the enzyme. From the model, the substrate binding cleft of the enzyme was redesigned in a manner that preferentially hydrolyzes glycans at specific glycosylation sites of triterpenoids. The designed mutants were shown to produce a variety of specialty triterpenoids with high purity. Rational design of a beta-glycosidase with high regiospecificity for triterpenoid tailoring.,Park SJ, Choi JM, Kyeong HH, Kim SG, Kim HS Chembiochem. 2015 Mar 23;16(5):854-60. doi: 10.1002/cbic.201500004. Epub 2015 Feb, 20. PMID:25703680 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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