5LIV
Crystal structure of myxobacterial CYP260A1
Summary for 5LIV
| Entry DOI | 10.2210/pdb5liv/pdb |
| Descriptor | Cytochrome P450 CYP260A1,Cytochrome P450 CYP260A1, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | 1-alpha-hydroxylase, steroid, sorangium cellulosum, redox pool, oxidoreductase |
| Biological source | Sorangium cellulosum So ce56 More |
| Total number of polymer chains | 4 |
| Total formula weight | 205042.82 |
| Authors | Carius, Y.,Khatri, Y.,Bernhardt, R.,Lancaster, C.R.D. (deposition date: 2016-07-15, release date: 2016-11-23, Last modification date: 2024-01-10) |
| Primary citation | Khatri, Y.,Carius, Y.,Ringle, M.,Lancaster, C.R.,Bernhardt, R. Structural characterization of CYP260A1 from Sorangium cellulosum to investigate the 1 alpha-hydroxylation of a mineralocorticoid. FEBS Lett., 590:4638-4648, 2016 Cited by PubMed Abstract: In this study, we report the crystal structure of the cytochrome P450 CYP260A1 (PDB 5LIV) from the myxobacterium Sorangium cellulosum So ce56. In addition, we investigated the hydroxylation of 11-deoxycorticosterone by CYP260A1 by reconstituting the enzyme with the surrogate redox partners adrenodoxin and adrenodoxin reductase. The major product of this steroid conversion was identified as 1α-hydroxy-11-deoxycorticosterone, a novel Δ4 C-21 steroidal derivative. Furthermore, we docked the substrate into the crystal structure and replaced Ser326, the residue responsible for substrate orientation, with asparagine and observed that the mutant S326N displayed higher activity and selectivity for the formation of 1α-hydroxy-11-deoxycorticosterone compared to the wild-type CYP260A1. Thus, our findings highlight the usefulness of the obtained crystal structure of CYP260A1 in identifying biotechnologically more efficient reactions. PubMed: 27878817DOI: 10.1002/1873-3468.12479 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.67 Å) |
Structure validation
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