2qbm | pdb_00002qbm

Crystal structure of the P450cam G248T mutant in the cyanide bound state

spinqualitylabelsall models 2qbm, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qbm is a 1 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CAM, CYN, HEM, K Related: 2qbl, 2qbn, 2qbo Gene: camC, cyp101 ("Bacillus fluorescens putidus" Flugge 1886) Activity: Camphor 5-monooxygenase, with EC number 1.14.15.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CPXA_PSEPU] Involved in a camphor oxidation system. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry.,Makris TM, von Koenig K, Schlichting I, Sligar SG Biochemistry. 2007 Dec 11;46(49):14129-40. Epub 2007 Nov 15. PMID:18001135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA