4N71

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

Summary for 4N71

• Entry DOI: 10.2210/pdb4n71/pdb
• Related: 4N6W
• Descriptor: Predicted HD phosphohydrolase PhnZ, FE (III) ION, [(1R)-2-amino-1-hydroxyethyl]phosphonic acid (3 entities in total)
• Functional Keywords: oxygenase, oxidoreductase
• Biological source: uncultured bacterium HF130_AEPn_1
• Total number of polymer chains: 4
• Total formula weight: 91764.64

Authors

Woersdoerfer, B.,Lingaraju, M.,Yennawar, N.,Boal, A.K.,Krebs, C.,Bollinger Jr, J.M.,Pandelia, M.-E. (deposition date: 2013-10-14, release date: 2013-11-27, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.984 Å)