TY - JOUR T1 - Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P JF - bioRxiv DO - 10.1101/116038 SP - 116038 AU - Ralph Krafczyk AU - Jakub Macošek AU - Daniel Gast AU - Swetlana Wunder AU - Pravin Kumar Ankush Jagtap AU - Prithiba Mitra AU - Amit Kumar Jha AU - Jüergen Rohr AU - Anja Hoffmann-Röeder AU - Kirsten Jung AU - Janosch Hennig AU - Jüergen Lassak Y1 - 2017/01/01 UR - http://biorxiv.org/content/early/2017/03/11/116038.abstract N2 - 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. ER -