5WXK

EarP bound with domain I of EF-P

5WXK の概要

• エントリーDOI: 10.2210/pdb5wxk/pdb
• 関連するPDBエントリー: 5WXI 5WXJ
• 分子名称: EarP, Elongation factor P, THYMIDINE-5'-DIPHOSPHATE, ... (8 entities in total)
• 機能のキーワード: glycosyltransferase, gt-b, ef-p, rhamnosylation, translation elongation, dtdp-rhamnose, transferase
• 由来する生物種: Neisseria meningitidis serogroup B / serotype 15 (strain H44/76); 詳細
• 細胞内の位置: Cytoplasm : E6MVW0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53261.65

構造登録者

Sengoku, T.,Yokoyama, S.,Yanagisawa, T. (登録日: 2017-01-07, 公開日: 2018-02-28, 最終更新日: 2024-04-03)

主引用文献

Sengoku, T.,Suzuki, T.,Dohmae, N.,Watanabe, C.,Honma, T.,Hikida, Y.,Yamaguchi, Y.,Takahashi, H.,Yokoyama, S.,Yanagisawa, T.
Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP
Nat. Chem. Biol., 14:368-374, 2018

PubMed Abstract: Protein glycosylation regulates many cellular processes. Numerous glycosyltransferases with broad substrate specificities have been structurally characterized. A novel inverting glycosyltransferase, EarP, specifically transfers rhamnose from dTDP-β-L-rhamnose to Arg32 of bacterial translation elongation factor P (EF-P) to activate its function. Here we report a crystallographic study of Neisseria meningitidis EarP. The EarP structure contains two tandem Rossmann-fold domains, which classifies EarP in glycosyltransferase superfamily B. In contrast to other structurally characterized protein glycosyltransferases, EarP binds the entire β-sheet structure of EF-P domain I through numerous interactions that specifically recognize its conserved residues. Thus Arg32 is properly located at the active site, and causes structural change in a conserved dTDP-β-L-rhamnose-binding loop of EarP. Rhamnosylation by EarP should occur via an S2 reaction, with Asp20 as the general base. The Arg32 binding and accompanying structural change of EarP may induce a change in the rhamnose-ring conformation suitable for the reaction.

PubMed: 29440735
DOI: 10.1038/s41589-018-0002-y

実験手法

X-RAY DIFFRACTION (1.801 Å)