5OMK
R2-like ligand-binding oxidase with aerobically reconstituted metal cofactor before photoconversion
Summary for 5OMK
| Entry DOI | 10.2210/pdb5omk/pdb |
| Related | 4HR0 4HR4 4HR5 4XB9 4XBV 4XBW 5DCO 5DCR 5DCS 5EKB 5OMJ |
| Descriptor | Ribonucleotide reductase small subunit, FE (III) ION, PALMITIC ACID, ... (4 entities in total) |
| Functional Keywords | r2-like ligand-binding oxidase, diiron cofactor, ribonucleotide reductase r2 subunit fold, metalloprotein oxidoreductase, oxidoreductase |
| Biological source | Geobacillus kaustophilus (strain HTA426) |
| Total number of polymer chains | 1 |
| Total formula weight | 37330.92 |
| Authors | Griese, J.J.,Hogbom, M. (deposition date: 2017-07-31, release date: 2018-01-03, Last modification date: 2024-01-17) |
| Primary citation | 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 Cited by 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: 29268610DOI: 10.1021/jacs.7b11966 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.704 Å) |
Structure validation
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