3L61
Crystal structure of substrate-free P450cam at 200 mM [K+]
Summary for 3L61
| Entry DOI | 10.2210/pdb3l61/pdb |
| Related | 3L62 3L63 |
| Descriptor | Camphor 5-monooxygenase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | cytochrome p450, p450cam, camphor, substrate-free, open conformation, metal-binding, monooxygenase, oxidoreductase |
| Biological source | Pseudomonas putida |
| Cellular location | Cytoplasm (By similarity): P00183 |
| Total number of polymer chains | 1 |
| Total formula weight | 47173.30 |
| Authors | Lee, Y.-T.,Wilson, R.F.,Rupniewski, I.,Goodin, D.B. (deposition date: 2009-12-22, release date: 2010-04-21, Last modification date: 2024-04-03) |
| Primary citation | Lee, Y.T.,Wilson, R.F.,Rupniewski, I.,Goodin, D.B. P450cam visits an open conformation in the absence of substrate. Biochemistry, 49:3412-3419, 2010 Cited by PubMed Abstract: P450cam from Pseudomonas putida is the best characterized member of the vast family of cytochrome P450s, and it has long been believed to have a more rigid and closed active site relative to other P450s. Here we report X-ray structures of P450cam crystallized in the absence of substrate and at high and low [K(+)]. The camphor-free structures are observed in a distinct open conformation characterized by a water-filled channel created by the retraction of the F and G helices, disorder of the B' helix, and loss of the K(+) binding site. Crystallization in the presence of K(+) alone does not alter the open conformation, while crystallization with camphor alone is sufficient for closure of the channel. Soaking crystals of the open conformation in excess camphor does not promote camphor binding or closure, suggesting resistance to conformational change by the crystal lattice. This open conformation is remarkably similar to that seen upon binding large tethered substrates, showing that it is not the result of a perturbation by the ligand. Redissolved crystals of the open conformation are observed as a mixture of P420 and P450 forms, which is converted to the P450 form upon addition of camphor and K(+). These data reveal that P450cam can dynamically visit an open conformation that allows access to the deeply buried active site without being induced by substrate or ligand. PubMed: 20297780DOI: 10.1021/bi100183g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
Download full validation report
