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- W2216093572 abstract "Structural and biochemical investigations of a xylosyltransferase in complex with a domain from its substrate Notch inform on the catalytic mechanism and the conformational rearrangements needed for substrate binding, while genetic analysis poses new questions in cancer biology. A major question remaining in glycobiology is how a glycosyltransferase (GT) that retains the anomeric linkage of a sugar catalyzes the reaction. Xyloside α-1,3-xylosyltransferase (XXYLT1) is a retaining GT that regulates Notch receptor activation by adding xylose to the Notch extracellular domain. Here, using natural acceptor and donor substrates and active Mus musculus XXYLT1, we report a series of crystallographic snapshots along the reaction, including an unprecedented natural and competent Michaelis reaction complex for retaining enzymes. These structures strongly support the SNi-like reaction as the retaining mechanism for XXYLT1. Unexpectedly, the epidermal growth factor–like repeat acceptor substrate undergoes a large conformational change upon binding to the active site, providing a structural basis for substrate specificity. Our improved understanding of this retaining enzyme will accelerate the design of retaining GT inhibitors that can modulate Notch activity in pathological situations in which Notch dysregulation is known to cause cancer or developmental disorders." @default.
- W2216093572 created "2016-06-24" @default.
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- W2216093572 date "2015-09-28" @default.
- W2216093572 modified "2023-09-30" @default.
- W2216093572 title "Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism" @default.
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- W2216093572 doi "https://doi.org/10.1038/nchembio.1927" @default.
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