Matches in SemOpenAlex for { <https://semopenalex.org/work/W2597267072> ?p ?o ?g. }
- W2597267072 abstract "ABSTRACT Glycosylation is a universal strategy to post-translationally modify proteins. The recently discovered arginine rhamnosylation activates the polyproline specific bacterial translation elongation factor EF-P. EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP. However, the enzymatic mechanism remains elusive. In the present study, we solved the crystal structure of EarP from Pseudomonas putida. The enzyme is composed of two opposing domains with Rossmann-folds, thus constituting a GT-B glycosyltransferase. While TDP-rhamnose is located within a highly conserved pocket of the C-domain, EarP recognizes the EF-P via its KOW-like N-domain. Based on our structural data combined with an in vitro /in vivo enzyme characterization, we propose a mechanism of inverting arginine glycosylation. As EarP is essential for pathogenicity in P. aeruginosa our study provides the basis for targeted inhibitor design." @default.
- W2597267072 created "2017-03-23" @default.
- W2597267072 creator A5005855579 @default.
- W2597267072 creator A5012863542 @default.
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- W2597267072 creator A5065874089 @default.
- W2597267072 creator A5073264375 @default.
- W2597267072 creator A5078790523 @default.
- W2597267072 date "2017-03-11" @default.
- W2597267072 modified "2023-10-14" @default.
- W2597267072 title "Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P" @default.
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