8GTL

Crystal Structure of Cytochrome P450 (CYP101D5)

Summary for 8GTL

• Entry DOI: 10.2210/pdb8gtl/pdb
• Descriptor: cytochrome P450 CYP101D5, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: ionone, cytochrome p450, chemical modification, heme oxidation, transferase
• Biological source: Sphingomonas echinoides
• Total number of polymer chains: 2
• Total formula weight: 92937.56

Authors

Do, H.,Lee, J.H. (deposition date: 2022-09-08, release date: 2022-12-28, Last modification date: 2023-11-29)

Primary citation

Subedi, P.,Do, H.,Lee, J.H.,Oh, T.J.
Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 from Sphingomonas echinoides.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: Cytochrome P450 enzymes (CYPs) are heme-containing enzymes that catalyze hydroxylation with a variety of biological molecules. Despite their diverse activity and substrates, the structures of CYPs are limited to a tertiary structure that is similar across all the enzymes. It has been presumed that CYPs overcome substrate selectivity with highly flexible loops and divergent sequences around the substrate entrance region. Here, we report the newly identified CYP101D5 from . CYP101D5 catalyzes the hydroxylation of β-ionone and flavonoids, including naringenin and apigenin, and causes the dehydrogenation of α-ionone. A structural investigation and comparison with other CYP101 families indicated that spatial constraints at the substrate-recognition site originate from the B/C loop. Furthermore, charge distribution at the substrate binding site may be important for substrate selectivity and the preference for CYP101D5.

PubMed: 36362105
DOI: 10.3390/ijms232113317

Experimental method

X-RAY DIFFRACTION (3.2 Å)