Structural highlights
7q9e is a 4 chain structure with sequence from Priestia megaterium DSM 319. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
D5DF35_PRIM3
Publication Abstract from PubMed
Understanding the structural basis of the selectivity of steroid hydroxylation requires detailed structural and functional investigations on various steroid hydroxylases with different selectivities, such as the bacterial cytochrome P450 enzymes. Here, the crystal structure of the cytochrome P450 CYP106A1 from Priestia megaterium was solved. CYP106A1 exhibits a rare additional structural motif of a cytochrome P450, a sixth beta-sheet. The protein was found in different unusual conformations corresponding to both open and closed forms even when crystallized without any known substrate. The structural comparison of CYP106A1 with the previously investigated CYP106A2, including docking studies for both isoforms with the substrate cortisol, reveals a completely different orientation of the steroid molecule in the active sites. This distinction convincingly explains the experimentally observed differences in substrate conversion and product formation by the two enzymes.
Structural comparison of the cytochrome P450 enzymes CYP106A1 and CYP106A2 provides insight into their differences in steroid conversion.,Carius Y, Hutter M, Kiss F, Bernhardt R, Lancaster CRD FEBS Lett. 2022 Sep 23. doi: 10.1002/1873-3468.14502. PMID:36151590[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carius Y, Hutter M, Kiss F, Bernhardt R, Lancaster CRD. Structural comparison of the cytochrome P450 enzymes CYP106A1 and CYP106A2 provides insight into their differences in steroid conversion. FEBS Lett. 2022 Sep 23. doi: 10.1002/1873-3468.14502. PMID:36151590 doi:http://dx.doi.org/10.1002/1873-3468.14502
