3iaa

Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP bound form

spinqualitylabelsall models 3iaa, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3iaa is a 2 chain structure with sequence from Atcc 15837. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TYD NonStd Res: MSE Related: 3ia7 Gene: calG2, Q8KNE0 (ATCC 15837) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Glycosyltransferases are useful synthetic catalysts for generating natural products with sugar moieties. Although several natural product glycosyltransferase structures have been reported, design principles of glycosyltransferase engineering for the generation of glycodiversified natural products has fallen short of its promise, partly due to a lack of understanding of the relationship between structure and function. Here, we report structures of all four calicheamicin glycosyltransferases (CalG1, CalG2, CalG3, and CalG4), whose catalytic functions are clearly regiospecific. Comparison of these four structures reveals a conserved sugar donor binding motif and the principles of acceptor binding region reshaping. Among them, CalG2 possesses a unique catalytic motif for glycosylation of hydroxylamine. Multiple glycosyltransferase structures in a single natural product biosynthetic pathway are a valuable resource for understanding regiospecific reactions and substrate selectivities and will help future glycosyltransferase engineering. Complete set of glycosyltransferase structures in the calicheamicin biosynthetic pathway reveals the origin of regiospecificity.,Chang A, Singh S, Helmich KE, Goff RD, Bingman CA, Thorson JS, Phillips GN Jr Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):17649-54. Epub 2011 Oct 10. PMID:21987796 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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