Alpha-(1,6)-fucosyltransferase Fut8 catalyses the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype []. Fut8 is also implicated to play roles in ageing []and cancer metastasis []. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear [].
Alpha-(1,6)-fucosyltransferase Fut8 catalyses the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype []. Fut8 is also implicated to play roles in ageing []and cancer metastasis []. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear []. This entry represents the SH3 domain of Fut8.
This domain includes the N-terminal coil-coiled domain and the catalytic domain of alpha-(1,6)-fucosyltransferase Fut8. The catalytic domain comprises two structures, an open sheet α/β structure, which contains five helices and three β-strands at the N-terminal, and a Rossmann fold that contains five helices and five β-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases [].Alpha-(1,6)-fucosyltransferase Fut8 catalyses the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype []. Fut8 is also implicated to play roles in ageing []and cancer metastasis []. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear [].
The fucosylation of glycoconjugates in mammalian organisms is related to awide variety of biological preocesses, including cell adhesion, blood antigens, and some severe diseases including cancer metastasis, congenital disorders of glycosylation, and various microbial and virus infections. Fucosylation via alpha1,2-, alpha1,3- alpha1,4, and alpha1,6-linkages, and protein O-fucosylation are accomplished by the cation of specific individual fucosyltransferases [].FUT8, a eukaryotic alpha1,6-fucosyltransferase, catalyses the transfer of afucosyl residue from guanine nucleotide diphosphate (GDP)-beta-L-fucose to thereducing terminal N-acetylglucosamine (GlcNAc) of asparagine-linkedoligosaccharides (N-glycan). The catalytic domain of FUT8 is structurallysimilar to that of BodZ, a bacterial alpha1,6-fucosyltransferase. NodZ plays arole in the synthesis of the Nod factor, which is involved in the nodulationof legume roots for nitrogen fixing, and is known to catalyse the alpha1,6-fucosylation of lipo-chitooligosaccharides and variations thereof, includingchitooligosaccharides. Both the eukaryotic and bacterial fucoslytransferaseare classified into the GT23 family of Carbohydrate-Active enZYmes and share GDP-beta-L-fucose as the donor substrate. Although the acceptor substrates are different, a "common"chitobiose unit is contained in the reducing terminals of both substrates [].The GT23 domain is comprised of two structures, a N-terminal open sheet alpha/beta structure and a C-terminal Rossmann fold which is frequently found innucleotide binding proteins including glycosyltransferases[, , ]. The entry represents the GT23 domain.
