9CJG
P450-G9 from Actinokineospora terrae, a non-canonical, serine-ligated cytochrome P450 in the ligand-free, closed conformation
Summary for 9CJG
| Entry DOI | 10.2210/pdb9cjg/pdb |
| Descriptor | Cytochrome P450-G9, PROTOPORPHYRIN IX CONTAINING FE, FORMIC ACID, ... (5 entities in total) |
| Functional Keywords | p450, cytochrome, serine, p411, oxidoreductase |
| Biological source | Actinokineospora terrae |
| Total number of polymer chains | 2 |
| Total formula weight | 90331.68 |
| Authors | |
| Primary citation | Nguy, A.K.L.,Ireland, K.A.,Kayrouz, C.M.,Caceres, J.C.,Greene, B.L.,Davis, K.M.,Seyedsayamdost, M.R. Non-Canonical Cytochrome P450 Enzymes in Nature. Biorxiv, 2024 Cited by PubMed Abstract: Cytochrome P450s (CYPs) are a superfamily of thiolate-ligated heme metalloenzymes principally responsible for the hydroxylation of unactivated C-H bonds. The lower-axial cysteine is an obligatory and universally conserved residue for the CYP enzyme class. Herein, we challenge this paradigm by systematically identifying non-canonical CYPs (ncCYPs) that do not harbor a cysteine ligand. Our bioinformatic search reveals 20 distinct ncCYP families with diverse ligands encoded in microbial genomes. We characterize a native serine-ligated CYP with a high-spin ferric resting state. Its crystal structure clearly shows a typical CYP fold and a serine alkoxide as a lower axial heme ligand. In addition, we report the discovery and characterization of the first native selenocysteine-ligated CYP in nature. Our findings radically expand the CYP metalloenzyme family. PubMed: 39763895DOI: 10.1101/2024.12.22.630014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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