2QBL
Crystal structure of ferric G248T cytochrome P450cam
Summary for 2QBL
| Entry DOI | 10.2210/pdb2qbl/pdb |
| Related | 2QBM 2QBN 2QBO |
| Descriptor | Cytochrome P450-cam, POTASSIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | cyp101, mutant, conserved active site residue, gly248, heme geometry, oxidoreductase |
| Biological source | Pseudomonas putida |
| Cellular location | Cytoplasm (By similarity): P00183 |
| Total number of polymer chains | 1 |
| Total formula weight | 48400.81 |
| Authors | von Koenig, K.,Makris, T.M.,Sligar, S.D.,Schlichting, I. (deposition date: 2007-06-18, release date: 2007-12-25, Last modification date: 2023-08-30) |
| Primary citation | Makris, T.M.,Koenig, K.V.,Schlichting, I.,Sligar, S.G. Alteration of P450 Distal Pocket Solvent Leads to Impaired Proton Delivery and Changes in Heme Geometry. Biochemistry, 46:14129-14140, 2007 Cited by PubMed Abstract: Distal pocket water molecules have been widely implicated in the delivery of protons required in O-O bond heterolysis in the P450 reaction cycle. Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket through mutagenesis of a distal pocket glycine to either valine or threonine results in the alteration of spin state equilibria, and has dramatic consequences on the catalytic rate, coupling efficiency, and kinetic solvent isotope effect parameters, highlighting an important role of the active-site hydration level on P450 catalysis. Cryoradiolysis of the mutant CYP101 oxyferrous complexes further indicates a specific perturbation of proton-transfer events required for the transformation of ferric-peroxo to ferric-hydroperoxo states. Finally, crystallography of the 248Val and 248Thr mutants in both the ferric camphor bound resting state and ferric-cyano adducts shows both the alteration of hydrogen-bonding networks and the alteration of heme geometry parameters. Taken together, these results indicate that the distal pocket microenvironment governs the transformation of reactive heme-oxygen intermediates in P450 cytochromes. PubMed: 18001135DOI: 10.1021/bi7013695 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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