1UED
Crystal Structure of OxyC a Cytochrome P450 Implicated in an Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis.
Summary for 1UED
| Entry DOI | 10.2210/pdb1ued/pdb |
| Related | 1lfk 1lg9 1lgf |
| Descriptor | P450 monooxygenase, PROTOPORPHYRIN IX CONTAINING FE, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | cytochrome p450 vancomycin biosynthesis, oxidoreductase |
| Biological source | Amycolatopsis orientalis |
| Total number of polymer chains | 2 |
| Total formula weight | 92324.42 |
| Authors | Pylypenko, O.,Vitali, F.,Zerbe, K.,Robinson, J.A.,Schlichting, I. (deposition date: 2003-05-11, release date: 2003-12-09, Last modification date: 2023-10-25) |
| Primary citation | Pylypenko, O.,Vitali, F.,Zerbe, K.,Robinson, J.A.,Schlichting, I. Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis J.Biol.Chem., 278:46727-46733, 2003 Cited by PubMed Abstract: Gene inactivation studies point to the involvement of OxyC in catalyzing the last oxidative phenol coupling reaction during glycopeptide antibiotic biosynthesis. Presently, the substrate and exact timing of the OxyC reaction are unknown. The substrate might be the bicyclic heptapeptide or a thioester derivative bound to a protein carrier domain. OxyC from the vancomycin producer Amycolatopsis orientalis was produced in Escherichia coli and crystallized, and its structure was determined to 1.9 A resolution. OxyC gave UV-visible spectra characteristic of a P450-like hemoprotein in the low spin ferric state. After reduction to the ferrous state by dithionite the CO-ligated form gave a 450-nm peak in a UV-difference spectrum. The addition of vancomycin aglycone to OxyC produced type I changes to the UV spectrum. OxyC exhibits the typical P450-fold, with the Cys ligand loop containing the signature sequence FGHGX-HXCLG and Cys-356 being the proximal axial thiolate ligand of the heme iron. The observation of a water molecule bound to the heme iron is consistent with the UV-visible spectra of OxyC indicating a low spin heme. A polyethylene glycol molecule occupying the active site might mimic the bicyclic heptapeptide substrate. Analysis of the structure of Oxy-proteins and other P450s indicates regions that might be involved in binding of the redox partner and possibly the protein carrier domain. PubMed: 12888556DOI: 10.1074/jbc.M306486200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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