5NV8

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

5NV8 の概要

• エントリーDOI: 10.2210/pdb5nv8/pdb
• 分子名称: EF-P arginine 32 rhamnosyl-transferase, 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE (3 entities in total)
• 機能のキーワード: glycosyltransferase, transferase
• 由来する生物種: Pseudomonas putida KT2440
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44226.52

構造登録者

Macosek, J.,Krafczyk, R.,Jagtap, P.K.A.,Lassaka, J.,Hennig, J. (登録日: 2017-05-03, 公開日: 2017-10-04, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.294 Å)