Structural basis for substrate specificity and catalysis of α1,6-fucosyltransferase.
Biocatalysis
Carbohydrate Sequence
Catalytic Domain
Crystallography, X-Ray
Fucosyltransferases
/ chemistry
Glycosylation
Guanosine Diphosphate
/ metabolism
Humans
Microarray Analysis
Models, Molecular
Polysaccharides
/ chemistry
Recombinant Proteins
/ chemistry
Substrate Specificity
src Homology Domains
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
20 02 2020
20 02 2020
Historique:
received:
05
01
2020
accepted:
30
01
2020
entrez:
22
2
2020
pubmed:
23
2
2020
medline:
6
5
2020
Statut:
epublish
Résumé
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 S
Identifiants
pubmed: 32080177
doi: 10.1038/s41467-020-14794-z
pii: 10.1038/s41467-020-14794-z
pmc: PMC7033129
doi:
Substances chimiques
Polysaccharides
0
Recombinant Proteins
0
Guanosine Diphosphate
146-91-8
Fucosyltransferases
EC 2.4.1.-
Glycoprotein 6-alpha-L-fucosyltransferase
EC 2.4.1.68
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
973Références
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