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Structural basis for substrate specificity and catalysis of α1,6-fucosyltransferase

Nat Commun. 2020; 
García-García A, Ceballos-Laita L, Serna S, Artschwager R, Reichardt NC, , Corzana F, Hurtado-Guerrero R, ,
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PCR Cloning and Subcloning Both the synthesis of the HsFUT8 construct and the engineered pHLSec together with the cloning of HsFUT8 into pHLSec-12His-GFP-TEV were performed by GenScript. Get A Quote

摘要

Core-fucosylation is an essential biological modification by which a fucose is transferred from GDP-β-L-fucose to the innermost N-acetylglucosamine residue of N-linked glycans. A single human enzyme α1,6-fucosyltransferase (FUT8) is the only enzyme responsible for this modification via the addition of an α-1,6-linked fucose to N-glycans. To date, the details of substrate recognition and catalysis by FUT8 remain unknown. Here, we report the crystal structure of FUT8 complexed with GDP and a biantennary complex N-glycan (G0), which provides insight into both substrate recognition and catalysis. FUT8 follows an SN2 mechanism and deploys a series of loops and an α-helix which all contribute in forming the bindi... More

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