7WEX
The crystal structure of substrate-free CYP107X1 from Streptomyces avermitilis
Summary for 7WEX
| Entry DOI | 10.2210/pdb7wex/pdb |
| Descriptor | Cytochrome P450 hydroxylase, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | cytochrome p450, substrate-free, oxidoreductase |
| Biological source | Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) |
| Total number of polymer chains | 1 |
| Total formula weight | 45404.45 |
| Authors | |
| Primary citation | Lin, S.,Ma, B.,Gao, Q.,Yang, J.,Lai, G.,Lin, R.,Yang, B.,Han, B.N.,Xu, L.H. The 16 alpha-Hydroxylation of Progesterone by Cytochrome P450 107X1 from Streptomyces avermitilis. Chem.Biodivers., 19:e202200177-e202200177, 2022 Cited by PubMed Abstract: Cytochrome P450 enzymes (CYPs or P450s) are ubiquitous heme-dependent enzymes that catalyze the monooxygenation of non-activated C-H bonds to modify the structure of the substrate. In this study, we heterologously expressed CYP107X1 from Streptomyces avermitilis and conducted in vitro substrate screening using the alternative redox partners putidaredoxin and putidaredoxin reductase. CYP107X1 catalyzed the 16α-hydroxylation of progesterone with regio- and stereoselectivity. The spectroscopic analyses showed that CYP107X1 bound progesterone with a relatively high K value of 65.3±38.9 μM. The K and k values for progesterone were estimated to be 47.7±12.0 μM and 0.30 min , respectively. Furthermore, a crystal structure was obtained of CYP107X1 bound with glycerol from the buffer solution. Interestingly, a conserved threonine was replaced with asparagine in CYP107X1, indicating that it may adopt an unnatural proton transfer process and play a crucial role in its catalytic activity. PubMed: 35426465DOI: 10.1002/cbdv.202200177 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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