8YHN

Crystal structure of Cytochrome P450 107P2 from streptomyces avermitilis

Summary for 8YHN

• Entry DOI: 10.2210/pdb8yhn/pdb
• Descriptor: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: cytochrome p450, monooxygenase, oxidoreductase
• Biological source: Streptomyces avermitilis
• Total number of polymer chains: 1
• Total formula weight: 46478.35

Authors

Jeong, E.S.,Kim, V.C.,Kim, C.M.,Lee, Y.B. (deposition date: 2024-02-28, release date: 2025-03-05, Last modification date: 2026-03-25)

Primary citation

Jeong, E.,Kim, V.,Kim, C.,Lee, Y.B.,Kim, D.
Structural Insights into the Interaction of Terpenoids with Streptomyces avermitilis CYP107P2.
Biomol Ther (Seoul), 32:474-480, 2024

PubMed Abstract: genome includes 33 genes encoding monooxygenation-catalyzing cytochrome P450 enzymes. We investigated the structure of CYP107P2 and its interactions with terpenoid compounds. The recombinant CYP107P2 protein was expressed in and the purified enzyme exhibited a typical P450 spectrum upon CO-binding in its reduced state. Type-I substrate-binding spectral titrations were observed with various terpenoid compounds, including α-pinene, β-pinene, α-terpinyl acetate, and (+)-3-carene. The calculated binding affinities () ranged from 15.9 to 50.8 μM. The X-ray crystal structure of CYP107P2 was determined at 1.99 Å resolution, with a well-conserved overall P450 folding conformation. The terpenoid compound docking models illustrated that the structural interaction between monoterpenes and CYP107P2, with the distance between heme and terpenes ranging from 3.4 to 5.4 Å, indicates potential substrate binding for P450 enzyme. This study suggests that CYP107P2 is a P450 enzyme capable of catalyzing terpenes as substrates, signifying noteworthy advancements in comprehending a novel P450 enzyme's involvement in terpene reactions.

PubMed: 38835149
DOI: 10.4062/biomolther.2024.045

Experimental method

X-RAY DIFFRACTION (1.986 Å)