7SOJ

Structure of V750A Soybean Lipoxygenase at 277K

7SOJ の概要

• エントリーDOI: 10.2210/pdb7soj/pdb
• 分子名称: Lipoxygenase, FE (III) ION (3 entities in total)
• 機能のキーワード: metal binding, lipid binding, oxidoreductase
• 由来する生物種: Glycine max (Soybean, Glycine hispida)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 189099.89

構造登録者

Gee, C.L.,Offenbacher, A.R.,Hu, S. (登録日: 2021-10-31, 公開日: 2022-11-02, 最終更新日: 2023-10-25)

主引用文献

Zaragoza, J.P.T.,Offenbacher, A.R.,Hu, S.,Gee, C.L.,Firestein, Z.M.,Minnetian, N.,Deng, Z.,Fan, F.,Iavarone, A.T.,Klinman, J.P.
Temporal and spatial resolution of distal protein motions that activate hydrogen tunneling in soybean lipoxygenase.
Proc.Natl.Acad.Sci.USA, 120:e2211630120-e2211630120, 2023

PubMed Abstract: The enzyme soybean lipoxygenase (SLO) provides a prototype for deep tunneling mechanisms in hydrogen transfer catalysis. This work combines room temperature X-ray studies with extended hydrogen-deuterium exchange experiments to define a catalytically-linked, radiating cone of aliphatic side chains that connects an active site iron center of SLO to the protein-solvent interface. Employing eight variants of SLO that have been appended with a fluorescent probe at the identified surface loop, nanosecond fluorescence Stokes shifts have been measured. We report a remarkable identity of the energies of activation () for the Stokes shifts decay rates and the millisecond C-H bond cleavage step that is restricted to side chain mutants within an identified thermal network. These findings implicate a direct coupling of distal protein motions surrounding the exposed fluorescent probe to active site motions controlling catalysis. While the role of dynamics in enzyme function has been predominantly attributed to a distributed protein conformational landscape, the presented data implicate a thermally initiated, cooperative protein reorganization that occurs on a timescale faster than nanosecond and represents the enthalpic barrier to the reaction of SLO.

PubMed: 36867685
DOI: 10.1073/pnas.2211630120

実験手法

X-RAY DIFFRACTION (1.85 Å)