6kj0

Bifunctional xylosidase/glucosidase LXYL mutant E529Q C2221

spinqualitylabelsall models 6kj0, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6kj0 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BKR, BMA, MAN, NAG, XYP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed LXYL-P1-2 is one of the few xylosidases that efficiently catalyze the reaction from 7-beta-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT), and is a potential enzyme used in Taxol industrial production. Here we report the crystal structure of LXYL-P1-2 and its XDT binding complex. These structures reveal an enzyme/product complex with the sugar conformation different from the enzyme/substrate complex reported previously in GH3 enzymes, even in the whole glycohydrolases family. In addition, the DT binding pocket is identified as the structural basis for the substrate specificity. Further structure analysis reveals common features in LXYL-P1-2 and Taxol binding protein tubulin, which might provide useful information for designing new Taxol carrier proteins for drug delivery. Structures of beta-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition.,Yang L, Chen TJ, Wang F, Li L, Yu WB, Si YK, Chen JJ, Liu WC, Zhu P, Gong W Commun Biol. 2020 Jan 10;3(1):22. doi: 10.1038/s42003-019-0744-4. PMID:31925310 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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