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Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P

Title data

Krafczyk, Ralph ; Macošek, Jakub ; Jagtap, Pravin Kumar Ankush ; Gast, Daniel ; Wunder, Swetlana ; Mitra, Prithiba ; Jha, Amit Kumar ; Rohr, Jürgen ; Hoffmann-Röder, Anja ; Jung, Kirsten ; Hennig, Janosch ; Lassak, Jürgen:
Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.
In: mBio. Vol. 8 (2017) Issue 5 .
ISSN 2150-7511
DOI: https://doi.org/10.1128/mBio.01412-17

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Pseudomonas aeruginosa; Pseudomonas putida; TDP-rhamnose; glycosylation; glycosyltransferase; nucleotide sugar; posttranslational modification; ribosomes; translation
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 07 Oct 2021 07:37
Last Modified: 07 Oct 2021 07:37
URI: https://eref.uni-bayreuth.de/id/eprint/67224