9CV8
Crystal Structure of Cytochrome P450 NysL bound to nystatin
This is a non-PDB format compatible entry.
Summary for 9CV8
| Entry DOI | 10.2210/pdb9cv8/pdb |
| Descriptor | NysL, PROTOPORPHYRIN IX CONTAINING FE, Nystatin, ... (5 entities in total) |
| Functional Keywords | cytochrome p450, nystatin, macrolide, oxidoreductase |
| Biological source | Streptomyces noursei |
| Total number of polymer chains | 2 |
| Total formula weight | 90291.09 |
| Authors | Murarka, V.C.,Poulos, T.L. (deposition date: 2024-07-28, release date: 2025-01-29, Last modification date: 2025-02-26) |
| Primary citation | Murarka, V.C.,Kim, J.S.,Lamb, D.C.,Kelly, S.L.,Poulos, T.L.,Follmer, A.H. Crystal structure of cytochrome P450 NysL and the structural basis for stereo- and regio-selective oxidation of antifungal macrolides. J.Biol.Chem., 301:108185-108185, 2025 Cited by PubMed Abstract: NysL, a cytochrome P450 monooxygenase from the Gram-positive bacterium Streptomyces noursei, catalyzes the C10 hydroxylation of 10-deoxynystain to nystatin A, a clinically important antifungal. In this study, we present the 2.0 Å resolution crystal structure of NysL bound to nystatin A. The structure of this complex provides key insights into the structural elements that dictate the regio- and stereo- selective oxidation of large 20-44-membered macrolide substrates. The closely related AmphL operates on a similar 38-member macrolide but oxidizes C8 rather than C10. This difference requires that the substrate for AmphL penetrate further into the active site relative to NysL. The depth of substrate penetration is controlled by interactions between an area of the substrate binding pocket deemed the "back-wall" and the hemiketal ring of the macrolide substrate. PubMed: 39814230DOI: 10.1016/j.jbc.2025.108185 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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