Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 09 2023
18 09 2023
Historique:
received:
18
05
2023
accepted:
24
08
2023
medline:
20
9
2023
pubmed:
19
9
2023
entrez:
18
9
2023
Statut:
epublish
Résumé
Soluble HMW1C-like N-glycosyltransferases (NGTs) catalyze the glycosylation of Asn residues in proteins, a process fundamental for bacterial autoaggregation, adhesion and pathogenicity. However, our understanding of their molecular mechanisms is hindered by the lack of structures of enzymatic complexes. Here, we report structures of binary and ternary NGT complexes of Aggregatibacter aphrophilus NGT (AaNGT), revealing an essential dyad of basic/acidic residues located in the N-terminal all α-domain (AAD) that intimately recognizes the Thr residue within the conserved motif Asn
Identifiants
pubmed: 37723184
doi: 10.1038/s41467-023-41238-1
pii: 10.1038/s41467-023-41238-1
pmc: PMC10507012
doi:
Substances chimiques
N-glycosyltransferase, Nocardia aerocolonigenes
EC 2.4.1.-
Bacterial Proteins
0
Asparagine
7006-34-0
Glucose
IY9XDZ35W2
Uridine Diphosphate
58-98-0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5785Informations de copyright
© 2023. Springer Nature Limited.
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