8HKJ

Crystal structure of the CYP102A5 haem Domain isolated from Bacillus cereus

Summary for 8HKJ

• Entry DOI: 10.2210/pdb8hkj/pdb
• Descriptor: Bifunctional cytochrome P450/NADPH--P450 reductase, PROTOPORPHYRIN IX CONTAINING FE, PALMITIC ACID (3 entities in total)
• Functional Keywords: cytochrome p450, monooxygenase, oxidoreductase
• Biological source: Bacillus cereus
• Total number of polymer chains: 12
• Total formula weight: 645581.77

Authors

Stanfield, J.K.,Onoda, H.,Sugimoto, H.,Shoji, O. (deposition date: 2022-11-27, release date: 2023-04-26, Last modification date: 2024-05-29)

Primary citation

Stanfield, J.K.,Onoda, H.,Ariyasu, S.,Kasai, C.,Burfoot, E.M.,Sugimoto, H.,Shoji, O.
Investigating the applicability of the CYP102A1-decoy-molecule system to other members of the CYP102A subfamily.
J.Inorg.Biochem., 245:112235-112235, 2023

PubMed Abstract: Cytochrome P450 enzymes (CYPs) have attracted much promise as biocatalysts in a push for cleaner and more environmentally friendly catalytic systems. However, changing the substrate specificity of CYPs, such as CYP102A1, can be a challenging task, requiring laborious mutagenesis. An alternative approach is the use of decoy molecules that "trick" the enzyme into becoming active by impersonating the native substrate. Whilst the decoy molecule system has been extensively developed for CYP102A1, its general applicability for other CYP102-family enzymes has yet to be shown. Herein, we demonstrate that decoy molecules can "trick" CYP102A5 and A7 into becoming active and hydroxylating non-native substrates. Furthermore, significant differences in decoy molecule selectivity as well as decoy molecule binding were observed. The X-ray crystal structure of the CYP102A5 haem domain was solved at 2.8 Å, delivering insight into a potential substate-binding site that differs significantly from CYP102A1.

PubMed: 37167731
DOI: 10.1016/j.jinorgbio.2023.112235

Experimental method

X-RAY DIFFRACTION (2.8 Å)