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

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 e...

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Autores principales:	Ralph Krafczyk, Jakub Macošek, Pravin Kumar Ankush Jagtap, Daniel Gast, Swetlana Wunder, Prithiba Mitra, Amit Kumar Jha, Jürgen Rohr, Anja Hoffmann-Röder, Kirsten Jung, Janosch Hennig, Jürgen Lassak
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2017
Materias:	Pseudomonas aeruginosa Pseudomonas putida TDP-rhamnose glycosylation glycosyltransferase nucleotide sugar Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/e5dfd8c25c524c26a390fbfaa6131228
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spelling	oai:doaj.org-article:e5dfd8c25c524c26a390fbfaa61312282021-11-15T15:51:51ZStructural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P10.1128/mBio.01412-172150-7511https://doaj.org/article/e5dfd8c25c524c26a390fbfaa61312282017-11-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01412-17https://doaj.org/toc/2150-7511ABSTRACT 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. 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.Ralph KrafczykJakub MacošekPravin Kumar Ankush JagtapDaniel GastSwetlana WunderPrithiba MitraAmit Kumar JhaJürgen RohrAnja Hoffmann-RöderKirsten JungJanosch HennigJürgen LassakAmerican Society for MicrobiologyarticlePseudomonas aeruginosaPseudomonas putidaTDP-rhamnoseglycosylationglycosyltransferasenucleotide sugarMicrobiologyQR1-502ENmBio, Vol 8, Iss 5 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Pseudomonas aeruginosa Pseudomonas putida TDP-rhamnose glycosylation glycosyltransferase nucleotide sugar Microbiology QR1-502
spellingShingle	Pseudomonas aeruginosa Pseudomonas putida TDP-rhamnose glycosylation glycosyltransferase nucleotide sugar Microbiology QR1-502 Ralph Krafczyk Jakub Macošek Pravin Kumar Ankush Jagtap Daniel Gast Swetlana Wunder Prithiba Mitra Amit Kumar Jha Jürgen Rohr Anja Hoffmann-Röder Kirsten Jung Janosch Hennig Jürgen Lassak Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
description	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. 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.
format	article
author	Ralph Krafczyk Jakub Macošek Pravin Kumar Ankush Jagtap Daniel Gast Swetlana Wunder Prithiba Mitra Amit Kumar Jha Jürgen Rohr Anja Hoffmann-Röder Kirsten Jung Janosch Hennig Jürgen Lassak
author_facet	Ralph Krafczyk Jakub Macošek Pravin Kumar Ankush Jagtap Daniel Gast Swetlana Wunder Prithiba Mitra Amit Kumar Jha Jürgen Rohr Anja Hoffmann-Röder Kirsten Jung Janosch Hennig Jürgen Lassak
author_sort	Ralph Krafczyk
title	Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
title_short	Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
title_full	Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
title_fullStr	Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
title_full_unstemmed	Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P
title_sort	structural basis for earp-mediated arginine glycosylation of translation elongation factor ef-p
publisher	American Society for Microbiology
publishDate	2017
url	https://doaj.org/article/e5dfd8c25c524c26a390fbfaa6131228
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Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P

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