5OMJ

R2-like ligand-binding oxidase with aerobically reconstituted metal cofactor after photoconversion

5OMJ の概要

• エントリーDOI: 10.2210/pdb5omj/pdb
• 関連するPDBエントリー: 4HR0 4HR4 4HR5 4XB9 4XBV 4XBW 5DCO 5DCR 5DCS 5EKB
• 分子名称: Ribonucleotide reductase small subunit, FE (III) ION, PALMITIC ACID, ... (4 entities in total)
• 機能のキーワード: r2-like ligand-binding oxidase, diiron cofactor, ribonucleotide reductase r2 subunit fold, metalloprotein oxidoreductase, oxidoreductase
• 由来する生物種: Geobacillus kaustophilus (strain HTA426)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37286.91

構造登録者

Griese, J.J.,Hogbom, M. (登録日: 2017-07-31, 公開日: 2018-01-03, 最終更新日: 2024-01-17)

主引用文献

Maugeri, P.T.,Griese, J.J.,Branca, R.M.,Miller, E.K.,Smith, Z.R.,Eirich, J.,Hogbom, M.,Shafaat, H.S.
Driving Protein Conformational Changes with Light: Photoinduced Structural Rearrangement in a Heterobimetallic Oxidase.
J. Am. Chem. Soc., 140:1471-1480, 2018

PubMed Abstract: The heterobimetallic R2lox protein binds both manganese and iron ions in a site-selective fashion and activates oxygen, ultimately performing C-H bond oxidation to generate a tyrosine-valine cross-link near the active site. In this work, we demonstrate that, following assembly, R2lox undergoes photoinduced changes to the active site geometry and metal coordination motif. Through spectroscopic, structural, and mass spectrometric characterization, the photoconverted species is found to consist of a tyrosinate-bound iron center following light-induced decarboxylation of a coordinating glutamate residue and cleavage of the tyrosine-valine cross-link. This process occurs with high quantum efficiencies (Φ = 3%) using violet and near-ultraviolet light, suggesting that the photodecarboxylation is initiated via ligand-to-metal charge transfer excitation. Site-directed mutagenesis and structural analysis suggest that the cross-linked tyrosine-162 is the coordinating residue. One primary product is observed following irradiation, indicating potential use of this class of proteins, which contains a putative substrate channel, for controlled photoinduced decarboxylation processes, with relevance for in vivo functionality of R2lox as well as application in environmental remediation.

PubMed: 29268610
DOI: 10.1021/jacs.7b11966

実験手法

X-RAY DIFFRACTION (2.005 Å)