5W75

Crystal Structure of Reconstructed Bacterial Elongation Factor Node 168

5W75 の概要

• エントリーDOI: 10.2210/pdb5w75/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: Elongation factor Tu, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, GUANOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: ancestral gene reconstruction, thermostability, ef-tu, asr, translation
• 由来する生物種: Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E)
• 細胞内の位置: Cytoplasm : B9K884
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 179927.88

構造登録者

Ortlund, E.A. (登録日: 2017-06-19, 公開日: 2018-04-25, 最終更新日: 2024-03-13)

主引用文献

Okafor, C.D.,Pathak, M.C.,Fagan, C.E.,Bauer, N.C.,Cole, M.F.,Gaucher, E.A.,Ortlund, E.A.
Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus.
Structure, 26:118-129.e3, 2018

PubMed Abstract: Rationally engineering thermostability in proteins would create enzymes and receptors that function under harsh industrial applications. Several sequence-based approaches can generate thermostable variants of mesophilic proteins. To gain insight into the mechanisms by which proteins become more stable, we use structural and dynamic analyses to compare two popular approaches, ancestral sequence reconstruction (ASR) and the consensus method, used to generate thermostable variants of Elongation Factor Thermo-unstable (EF-Tu). We present crystal structures of ancestral and consensus EF-Tus, accompanied by molecular dynamics simulations aimed at probing the strategies employed to enhance thermostability. All proteins adopt crystal structures similar to extant EF-Tus, revealing no difference in average structure between the methods. Molecular dynamics reveals that ASR-generated sequences retain dynamic properties similar to extant, thermostable EF-Tu from Thermus aquaticus, while consensus EF-Tu dynamics differ from evolution-based sequences. This work highlights the advantage of ASR for engineering thermostability while preserving natural motions in multidomain proteins.

PubMed: 29276038
DOI: 10.1016/j.str.2017.11.018

実験手法

X-RAY DIFFRACTION (2.298 Å)