6VU0

CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FROM THE ESCHERICHIA COLI ENZYME

6VU0 の概要

• エントリーDOI: 10.2210/pdb6vu0/pdb
• 関連するPDBエントリー: 6V9K 6VBJ
• 分子名称: PEP-protein phosphotransferase system enzyme I, SULFATE ION (2 entities in total)
• 機能のキーワード: phosphoenolpyruvate-protein phosphotransferase ptsi, enzyme i, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70893.26

構造登録者

Stewart Jr., C.E. (登録日: 2020-02-14, 公開日: 2020-06-17, 最終更新日: 2023-10-11)

主引用文献

Dotas, R.R.,Nguyen, T.T.,Stewart Jr., C.E.,Ghirlando, R.,Potoyan, D.A.,Venditti, V.
Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.
J.Mol.Biol., 432:4481-4498, 2020

PubMed Abstract: Conformational disorder is emerging as an important feature of biopolymers, regulating a vast array of cellular functions, including signaling, phase separation, and enzyme catalysis. Here we combine NMR, crystallography, computer simulations, protein engineering, and functional assays to investigate the role played by conformational heterogeneity in determining the activity of the C-terminal domain of bacterial Enzyme I (EIC). In particular, we design chimeric proteins by hybridizing EIC from thermophilic and mesophilic organisms, and we characterize the resulting constructs for structure, dynamics, and biological function. We show that EIC exists as a mixture of active and inactive conformations and that functional regulation is achieved by tuning the thermodynamic balance between active and inactive states. Interestingly, we also present a hybrid thermophilic/mesophilic enzyme that is thermostable and more active than the wild-type thermophilic enzyme, suggesting that hybridizing thermophilic and mesophilic proteins is a valid strategy to engineer thermostable enzymes with significant low-temperature activity.

PubMed: 32504625
DOI: 10.1016/j.jmb.2020.05.024

実験手法

X-RAY DIFFRACTION (3.5 Å)