5nv8
Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P
Structural highlights
FunctionEARP_PSEPK Protein-arginine rhamnosyltransferase that catalyzes the transfer of a single rhamnose to elongation factor P (EF-P) on 'Lys-32', a modification required for EF-P-dependent rescue of polyproline stalled ribosomes.[1] Publication Abstract from PubMedGlycosylation 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-beta-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. Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.,Krafczyk R, Macosek J, Jagtap PKA, Gast D, Wunder S, Mitra P, Jha AK, Rohr J, Hoffmann-Roder A, Jung K, Hennig J, Lassak J MBio. 2017 Sep 26;8(5). pii: e01412-17. doi: 10.1128/mBio.01412-17. PMID:28951478[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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