7Q9E

CYP106A1

Summary for 7Q9E

• Entry DOI: 10.2210/pdb7q9e/pdb
• Related: 4YT3
• Descriptor: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (9 entities in total)
• Functional Keywords: cytochrome p450, steroid dehydrogenation, biosynthetic protein
• Biological source: Bacillus megaterium (strain DSM 319)
• Total number of polymer chains: 4
• Total formula weight: 198507.98

Authors

Carius, Y.,Hutter, M.,Kiss, F.,Bernhardt, R.,Lancaster, C.R.D. (deposition date: 2021-11-12, release date: 2022-10-19, Last modification date: 2024-01-31)

Primary citation

Carius, Y.,Hutter, M.,Kiss, F.,Bernhardt, R.,Lancaster, C.R.D.
Structural comparison of the cytochrome P450 enzymes CYP106A1 and CYP106A2 provides insight into their differences in steroid conversion.
Febs Lett., 596:3133-3144, 2022

PubMed Abstract: 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 β-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.

PubMed: 36151590
DOI: 10.1002/1873-3468.14502

Experimental method

X-RAY DIFFRACTION (1.7 Å)