RT Journal Article
SR Electronic
T1 Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 116038
DO 10.1101/116038
A1 Ralph Krafczyk
A1 Jakub Macošek
A1 Daniel Gast
A1 Swetlana Wunder
A1 Pravin Kumar Ankush Jagtap
A1 Prithiba Mitra
A1 Amit Kumar Jha
A1 Jürgen Rohr
A1 Anja Hoffmann-Röeder
A1 Kirsten Jung
A1 Janosch Hennig
A1 Jürgen Lassak
YR 2017
UL http://biorxiv.org/content/early/2017/03/13/116038.abstract
AB 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.