9OEV

HalA I151N with lysine, succinate, chloride, and vanadium(IV)-oxo

9OEV の概要

• エントリーDOI: 10.2210/pdb9oev/pdb
• 分子名称: Lysine halogenase, LYSINE, SUCCINIC ACID, ... (7 entities in total)
• 機能のキーワード: halogenase, fe/2og oxidase, biosynthetic protein
• 由来する生物種: Actinoplanes teichomyceticus
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 241420.78

構造登録者

Kissman, E.N.,Chang, M.C.Y. (登録日: 2025-04-29, 公開日: 2025-11-19, 最終更新日: 2025-12-03)

主引用文献

Kissman, E.N.,Kipouros, I.,Slater, J.W.,Stone, E.A.,Yang, A.Y.,Braun, A.,Ensberg, A.R.,Whitten, A.M.,Chatterjee, K.,Bogacz, I.,Yano, J.,Martin Bollinger Jr., J.,Chang, M.C.Y.
Dynamic metal coordination controls chemoselectivity in a radical halogenase.
Nat.Chem.Biol., 2025

PubMed Abstract: The activation of inert C(sp)-H bonds by nonheme Fe enzymes provides a powerful biocatalytic platform for the chemical synthesis of molecules with increased sp complexity. In this context, Fe/α-ketoglutarate-dependent radical halogenases are uniquely capable of carrying out transfer of a diverse array of bound anions following C-H activation. Here, we provide experimental evidence that bifurcation of radical rebound after H-atom abstraction can be driven both by the ability of a dynamic metal coordination sphere to reorganize and by a second-sphere hydrogen-bonding network where only two residues are sufficient. In addition, we present crystallographic data supporting the existence of an early peroxyhemiketal intermediate in the O activation pathway of Fe/α-ketoglutarate-dependent enzymes. These data provide a paradigm for understanding the evolution of catalytic plasticity in these enzymes and yields insight into the design principles by which to expand their reaction scope.

PubMed: 41272319
DOI: 10.1038/s41589-025-02077-x

実験手法

X-RAY DIFFRACTION (2.17 Å)