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Landomycin Glycosyltransferase LanGT2
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Structural highlights
FunctionPublication Abstract from PubMedThe structures of the O-glycosyltransferase LanGT2 and the engineered, CC bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates. Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2.,Tam HK, Harle J, Gerhardt S, Rohr J, Wang G, Thorson JS, Bigot A, Lutterbeck M, Seiche W, Breit B, Bechthold A, Einsle O Angew Chem Int Ed Engl. 2015 Jan 7. doi: 10.1002/anie.201409792. PMID:25581707[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 17:50, 20 September 2023.