7APM

tRNA-guanine transglycosylase H319C mutant spin-labeled with MTSL.

7APM の概要

• エントリーDOI: 10.2210/pdb7apm/pdb
• 関連するPDBエントリー: 7APL
• 分子名称: Queuine tRNA-ribosyltransferase, ZINC ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: enzyme, spin label, transferase
• 由来する生物種: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43564.12

構造登録者

Nguyen, D.,Heine, A.,Klebe, G. (登録日: 2020-10-18, 公開日: 2020-10-28, 最終更新日: 2024-01-31)

主引用文献

Nguyen, D.,Abdullin, D.,Heubach, C.A.,Pfaffeneder, T.,Nguyen, A.,Heine, A.,Reuter, K.,Diederich, F.,Schiemann, O.,Klebe, G.
Unraveling a Ligand-Induced Twist of a Homodimeric Enzyme by Pulsed Electron-Electron Double Resonance.
Angew.Chem.Int.Ed.Engl., 60:23419-23426, 2021

PubMed Abstract: Mechanistic insights into protein-ligand interactions can yield chemical tools for modulating protein function and enable their use for therapeutic purposes. For the homodimeric enzyme tRNA-guanine transglycosylase (TGT), a putative virulence target of shigellosis, ligand binding has been shown by crystallography to transform the functional dimer geometry into an incompetent twisted one. However, crystallographic observation of both end states does neither verify the ligand-induced transformation of one dimer into the other in solution nor does it shed light on the underlying transformation mechanism. We addressed these questions in an approach that combines site-directed spin labeling (SDSL) with distance measurements based on pulsed electron-electron double resonance (PELDOR or DEER) spectroscopy. We observed an equilibrium between the functional and twisted dimer that depends on the type of ligand, with a pyranose-substituted ligand being the most potent one in shifting the equilibrium toward the twisted dimer. Our experiments suggest a dissociation-association mechanism for the formation of the twisted dimer upon ligand binding.

PubMed: 34387025
DOI: 10.1002/anie.202108179

実験手法

X-RAY DIFFRACTION (1.66 Å)