6F6F
R2-like ligand-binding oxidase V72I mutant with aerobically reconstituted Mn/Fe cofactor
Summary for 6F6F
| Entry DOI | 10.2210/pdb6f6f/pdb |
| Related | 4HR0 4HR4 4HR5 4XB9 4XBV 4XBW 5DCO 5DCR 5DCS 5EKB 5OMJ 5OMK 6F65 6F6B 6F6C 6F6E 6F6G 6F6H 6F6K 6F6L 6F6M |
| Descriptor | Ribonucleotide reductase small subunit, PALMITIC ACID, MANGANESE (III) ION, ... (6 entities in total) |
| Functional Keywords | r2-like ligand-binding oxidase, mn/fe cofactor, ribonucleotide reductase r2 subunit fold, metalloprotein oxidoreductase, oxidoreductase |
| Biological source | Geobacillus kaustophilus (strain HTA426) |
| Total number of polymer chains | 1 |
| Total formula weight | 37398.98 |
| Authors | Griese, J.J.,Hogbom, M. (deposition date: 2017-12-05, release date: 2018-07-04, Last modification date: 2024-01-17) |
| Primary citation | Griese, J.J.,Branca, R.M.M.,Srinivas, V.,Hogbom, M. Ether cross-link formation in the R2-like ligand-binding oxidase. J. Biol. Inorg. Chem., 23:879-886, 2018 Cited by PubMed Abstract: R2-like ligand-binding oxidases contain a dinuclear metal cofactor which can consist either of two iron ions or one manganese and one iron ion, but the heterodinuclear Mn/Fe cofactor is the preferred assembly in the presence of Mn and Fe in vitro. We have previously shown that both types of cofactor are capable of catalyzing formation of a tyrosine-valine ether cross-link in the protein scaffold. Here we demonstrate that Mn/Fe centers catalyze cross-link formation more efficiently than Fe/Fe centers, indicating that the heterodinuclear cofactor is the biologically relevant one. We further explore the chemical potential of the Mn/Fe cofactor by introducing mutations at the cross-linking valine residue. We find that cross-link formation is possible also to the tertiary beta-carbon in an isoleucine, but not to the secondary beta-carbon or tertiary gamma-carbon in a leucine, nor to the primary beta-carbon of an alanine. These results illustrate that the reactivity of the cofactor is highly specific and directed. PubMed: 29946980DOI: 10.1007/s00775-018-1583-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.788 Å) |
Structure validation
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