8GAR
Nitrosomonas europaea Cytochrome P460 Arg44Ala
Summary for 8GAR
| Entry DOI | 10.2210/pdb8gar/pdb |
| Descriptor | Cytochrome P460, HEME C, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | cytochrome, heme protein, metal binding protein |
| Biological source | Nitrosomonas europaea |
| Total number of polymer chains | 1 |
| Total formula weight | 21914.54 |
| Authors | Bollmeyer, M.M.,Lancaster, K.M. (deposition date: 2023-02-23, release date: 2023-07-05, Last modification date: 2024-10-30) |
| Primary citation | Bollmeyer, M.M.,Coleman, R.E.,Majer, S.H.,Ferrao, S.D.,Lancaster, K.M. Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification. J.Am.Chem.Soc., 145:14404-14416, 2023 Cited by PubMed Abstract: Cytochrome P460s are heme enzymes that oxidize hydroxylamine to nitrous oxide. They bear specialized "heme P460" cofactors that are cross-linked to their host polypeptides by a post-translationally modified lysine residue. Wild-type cytochrome P460 may be isolated as a cross-link-deficient proenzyme following anaerobic overexpression in . When treated with peroxide, this proenzyme undergoes maturation to active enzyme with spectroscopic and catalytic properties that match wild-type cyt P460. This maturation reactivity requires no chaperones─it is intrinsic to the protein. This behavior extends to the broader cytochrome c' superfamily. Accumulated data reveal key contributions from the secondary coordination sphere that enable selective, complete maturation. Spectroscopic data support the intermediacy of a ferryl species along the maturation pathway. PubMed: 37338957DOI: 10.1021/jacs.3c03608 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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