4N71

X-Ray Crystal Structure of 2-amino-1-hydroxyethylphosphonate-bound PhnZ

4N71 の概要

• エントリーDOI: 10.2210/pdb4n71/pdb
• 関連するPDBエントリー: 4N6W
• 分子名称: Predicted HD phosphohydrolase PhnZ, FE (III) ION, [(1R)-2-amino-1-hydroxyethyl]phosphonic acid (3 entities in total)
• 機能のキーワード: oxygenase, oxidoreductase
• 由来する生物種: uncultured bacterium HF130_AEPn_1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 91764.64

構造登録者

Woersdoerfer, B.,Lingaraju, M.,Yennawar, N.,Boal, A.K.,Krebs, C.,Bollinger Jr, J.M.,Pandelia, M.-E. (登録日: 2013-10-14, 公開日: 2013-11-27, 最終更新日: 2024-02-28)

主引用文献

Worsdorfer, B.,Lingaraju, M.,Yennawar, N.H.,Boal, A.K.,Krebs, C.,Bollinger, J.M.,Pandelia, M.E.
Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases.
Proc.Natl.Acad.Sci.USA, 110:18874-18879, 2013

PubMed Abstract: The founding members of the HD-domain protein superfamily are phosphohydrolases, and newly discovered members are generally annotated as such. However, myo-inositol oxygenase (MIOX) exemplifies a second, very different function that has evolved within the common scaffold of this superfamily. A recently discovered HD protein, PhnZ, catalyzes conversion of 2-amino-1-hydroxyethylphosphonate to glycine and phosphate, culminating a bacterial pathway for the utilization of environmentally abundant 2-aminoethylphosphonate. Using Mössbauer and EPR spectroscopies, X-ray crystallography, and activity measurements, we show here that, like MIOX, PhnZ employs a mixed-valent Fe(II)/Fe(III) cofactor for the O2-dependent oxidative cleavage of its substrate. Phylogenetic analysis suggests that many more HD proteins may catalyze yet-unknown oxygenation reactions using this hitherto exceptional Fe(II)/Fe(III) cofactor. The results demonstrate that the catalytic repertoire of the HD superfamily extends well beyond phosphohydrolysis and suggest that the mechanism used by MIOX and PhnZ may be a common strategy for oxidative C-X bond cleavage.

PubMed: 24198335
DOI: 10.1073/pnas.1315927110

実験手法

X-RAY DIFFRACTION (2.984 Å)