Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
Open Access
- 8 November 2017
- journal article
- research article
- Published by American Society for Microbiology in mBio
- Vol. 8 (5), e01412-17
- https://doi.org/10.1128/mbio.01412-17
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.Keywords
Funding Information
- European Molecular Biology Laboratory
- Center for Integrated Protein Science Munich
- EU Marie Curie Actions Cofund for an EIPOD Fellowship
- HHS | National Institutes of Health (# GM 105977)
- Deutsche Forschungsgemeinschaft (LA 3658/1-1)
- Deutsche Forschungsgemeinschaft (GRK2062)
This publication has 106 references indexed in Scilit:
- PoxA, YjeK, and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in Salmonella entericaMolecular Cell, 2010
- I-TASSER: a unified platform for automated protein structure and function predictionNature Protocols, 2010
- TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shiftsJournal of Biomolecular NMR, 2009
- Protein structure prediction on the Web: a case study using the Phyre serverNature Protocols, 2009
- Version 1.2 of the Crystallography and NMR systemNature Protocols, 2007
- UCSF Chimera?A visualization system for exploratory research and analysisJournal of Computational Chemistry, 2004
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970