Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P

Ralph Krafczyk, Jakub Macošek, Pravin Kumar Ankush Jagtap, Daniel Gast, Swetlana Wunder, Prithiba Mitra, Amit Kumar Jha, Jürgen Rohr, Anja Hoffmann-Röder, Kirsten Jung, Janosch Hennig, Jürgen Lassak

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Glycosylation is a universal strategy to posttranslationally 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 B pattern-type glycosyltransferase (GT-B). While dTDP-β-L-rhamnose is located within a highly conserved pocket of the C-domain, EarP recognizes the KOW-like N-domain of EF-P. Based on our data, we propose a structural model for arginine glycosylation by EarP. As EarP is essential for pathogenicity in P. aeruginosa, our study provides the basis for targeted inhibitor design. IMPORTANCE The structural and biochemical characterization of the EF-P-specific rhamnosyltransferase EarP not only provides the first molecular insights into arginine glycosylation but also lays the basis for targeted-inhibitor design against Pseudomonas aeruginosa infection.

Original languageEnglish
Article numbere01412-17
JournalmBio
Volume8
Issue number5
DOIs
StatePublished - Sep 1 2017

Bibliographical note

Publisher Copyright:
© 2017 Krafczyk et al.

Keywords

  • Glycosylation
  • Glycosyltransferase
  • Nucleotide sugar
  • Posttranslational modification
  • Pseudomonas aeruginosa
  • Pseudomonas putida
  • Ribosomes
  • TDP-rhamnose
  • Translation

ASJC Scopus subject areas

  • Microbiology
  • Virology

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