Matches in SemOpenAlex for { <https://semopenalex.org/work/W3080991129> ?p ?o ?g. }
- W3080991129 abstract "Acyltransferase-3 (AT3) domain-containing membrane proteins are involved in O -acetylation of a diverse range of carbohydrates across all domains of life. In bacteria they are essential in processes including symbiosis, resistance to antimicrobials, and biosynthesis of antibiotics. Their mechanism of action, however, is poorly characterized. We analyzed two acetyltransferases as models for this important family of membrane proteins, which modify carbohydrates on the surface of the pathogen Salmonella enterica , affecting immunogenicity, virulence, and bacteriophage resistance. We show that when these AT3 domains are fused to a periplasmic partner domain, both domains are required for substrate acetylation. The data show conserved elements in the AT3 domain and unique structural features of the periplasmic domain. Our data provide a working model to probe the mechanism and function of the diverse and important members of the widespread AT3 protein family, which are required for biologically significant modifications of cell-surface carbohydrates." @default.
- W3080991129 created "2020-09-01" @default.
- W3080991129 creator A5017245212 @default.
- W3080991129 creator A5024108011 @default.
- W3080991129 creator A5045297162 @default.
- W3080991129 creator A5053309845 @default.
- W3080991129 creator A5059430118 @default.
- W3080991129 creator A5071488584 @default.
- W3080991129 creator A5073227677 @default.
- W3080991129 creator A5088148254 @default.
- W3080991129 date "2020-08-25" @default.
- W3080991129 modified "2023-10-09" @default.
- W3080991129 title "Acetylation of Surface Carbohydrates in Bacterial Pathogens Requires Coordinated Action of a Two-Domain Membrane-Bound Acyltransferase" @default.
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