5NV8

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

Summary for 5NV8

• Entry DOI: 10.2210/pdb5nv8/pdb
• Descriptor: EF-P arginine 32 rhamnosyl-transferase, 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE (3 entities in total)
• Functional Keywords: glycosyltransferase, transferase
• Biological source: Pseudomonas putida KT2440
• Total number of polymer chains: 1
• Total formula weight: 44226.52

Authors

Macosek, J.,Krafczyk, R.,Jagtap, P.K.A.,Lassaka, J.,Hennig, J. (deposition date: 2017-05-03, release date: 2017-10-04, Last modification date: 2024-05-08)

Primary citation

Krafczyk, R.,Macosek, J.,Jagtap, P.K.A.,Gast, D.,Wunder, S.,Mitra, P.,Jha, A.K.,Rohr, J.,Hoffmann-Roder, A.,Jung, K.,Hennig, J.,Lassak, J.
Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.
MBio, 8:-, 2017

PubMed 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 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 , our study provides the basis for targeted inhibitor design. 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 infection.

PubMed: 28951478
DOI: 10.1128/mBio.01412-17

Experimental method

X-RAY DIFFRACTION (2.294 Å)