Structural highlights
5liv is a 4 chain structure with sequence from Sorangium cellulosum So ce56. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.67Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A9FDB7_SORC5
Publication Abstract from PubMed
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 1alpha-hydroxy-11-deoxycorticosterone, a novel Delta4 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 1alpha-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.
Structural characterization of CYP260A1 from Sorangium cellulosum to investigate the 1alpha-hydroxylation of a mineralocorticoid.,Khatri Y, Carius Y, Ringle M, Lancaster CR, Bernhardt R FEBS Lett. 2016 Nov 7. doi: 10.1002/1873-3468.12479. PMID:27878817[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Khatri Y, Carius Y, Ringle M, Lancaster CR, Bernhardt R. Structural characterization of CYP260A1 from Sorangium cellulosum to investigate the 1alpha-hydroxylation of a mineralocorticoid. FEBS Lett. 2016 Nov 7. doi: 10.1002/1873-3468.12479. PMID:27878817 doi:http://dx.doi.org/10.1002/1873-3468.12479
