6ALM

VioC L-arginine hydroxylase bound to Fe(II), L-arginine, and 2-OXO-GLUTARIC ACID

6ALM の概要

• エントリーDOI: 10.2210/pdb6alm/pdb
• 分子名称: Alpha-ketoglutarate-dependent L-arginine hydroxylase, FE (II) ION, 2-OXOGLUTARIC ACID, ... (5 entities in total)
• 機能のキーワード: hydroxylase, 2-oxo-glutarate, iron, oxidoreductase
• 由来する生物種: Streptomyces vinaceus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43687.57

構造登録者

Dunham, N.P.,Mitchell, A.J.,Boal, A.K. (登録日: 2017-08-08, 公開日: 2017-09-06, 最終更新日: 2023-10-04)

主引用文献

Mitchell, A.J.,Dunham, N.P.,Martinie, R.J.,Bergman, J.A.,Pollock, C.J.,Hu, K.,Allen, B.D.,Chang, W.C.,Silakov, A.,Bollinger, J.M.,Krebs, C.,Boal, A.K.
Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase.
J. Am. Chem. Soc., 139:13830-13836, 2017

PubMed Abstract: Iron(II)- and 2-(oxo)-glutarate-dependent oxygenases catalyze diverse oxidative transformations that are often initiated by abstraction of hydrogen from carbon by iron(IV)-oxo (ferryl) complexes. Control of the relative orientation of the substrate C-H and ferryl Fe-O bonds, primarily by direction of the oxo group into one of two cis-related coordination sites (termed inline and offline), may be generally important for control of the reaction outcome. Neither the ferryl complexes nor their fleeting precursors have been crystallographically characterized, hindering direct experimental validation of the offline hypothesis and elucidation of the means by which the protein might dictate an alternative oxo position. Comparison of high-resolution X-ray crystal structures of the substrate complex, an Fe(II)-peroxysuccinate ferryl precursor, and a vanadium(IV)-oxo mimic of the ferryl intermediate in the l-arginine 3-hydroxylase, VioC, reveals coordinated motions of active site residues that appear to control the intermediate geometries to determine reaction outcome.

PubMed: 28823155
DOI: 10.1021/jacs.7b07374

実験手法

X-RAY DIFFRACTION (1.6 Å)