6QI1

Time resolved structural analysis of the full turnover of an enzyme - 12312 ms

6QI1 の概要

• エントリーDOI: 10.2210/pdb6qi1/pdb
• 分子名称: Fluoroacetate dehalogenase, fluoroacetic acid (3 entities in total)
• 機能のキーワード: time-resolved, catalysis, intermediate, hydrolase
• 由来する生物種: Rhodopseudomonas palustris
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68225.36

構造登録者

Schulz, E.C.,Mehrabi, P.,Pai, E.F.,Miller, D. (登録日: 2019-01-17, 公開日: 2019-09-25, 最終更新日: 2024-05-15)

主引用文献

Mehrabi, P.,Schulz, E.C.,Dsouza, R.,Muller-Werkmeister, H.M.,Tellkamp, F.,Miller, R.J.D.,Pai, E.F.
Time-resolved crystallography reveals allosteric communication aligned with molecular breathing.
Science, 365:1167-1170, 2019

PubMed Abstract: A comprehensive understanding of protein function demands correlating structure and dynamic changes. Using time-resolved serial synchrotron crystallography, we visualized half-of-the-sites reactivity and correlated molecular-breathing motions in the enzyme fluoroacetate dehalogenase. Eighteen time points from 30 milliseconds to 30 seconds cover four turnover cycles of the irreversible reaction. They reveal sequential substrate binding, covalent-intermediate formation, setup of a hydrolytic water molecule, and product release. Small structural changes of the protein mold and variations in the number and placement of water molecules accompany the various chemical steps of catalysis. Triggered by enzyme-ligand interactions, these repetitive changes in the protein framework's dynamics and entropy constitute crucial components of the catalytic machinery.

PubMed: 31515393
DOI: 10.1126/science.aaw9904

実験手法

X-RAY DIFFRACTION (1.9 Å)