3h4i

Chimeric Glycosyltransferase for the generation of novel natural products

spinqualitylabelsall models 3h4i, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3h4i is a 1 chain structure with sequence from "actinoplanes_teichomyceticus"_parenti_et_al._1978 "actinoplanes teichomyceticus" parenti et al. 1978. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, U2F Related: 3h4t Gene: GtfA ("Actinoplanes teichomyceticus" Parenti et al. 1978) 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 Glycodiversification, an invaluable tool for generating biochemical diversity, can be catalyzed by glycosyltransferases, which attach activated sugar "donors" onto "acceptor" molecules. However, many glycosyltransferases can tolerate only minor modifications to their native substrates, thus making them unsuitable tools for current glycodiversification strategies. Here we report the production of functional chimeric glycosyltransferases by mixing and matching the N- and C-terminal domains of glycopeptide glycosyltransferases. Using this method we have generated hybrid glycopeptides and have demonstrated that domain swapping can result in a predictable switch of substrate specificity, illustrating that N- and C-terminal domains predominantly dictate acceptor and donor specificity, respectively. The determination of the structure of a chimera in complex with a sugar donor analog shows that almost all sugar-glycosyltransferase binding interactions occur in the C-terminal domain. Chimeric glycosyltransferases for the generation of hybrid glycopeptides.,Truman AW, Dias MV, Wu S, Blundell TL, Huang F, Spencer JB Chem Biol. 2009 Jun 26;16(6):676-85. PMID:19549605 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycosyltransferase

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