3fwg

Ferric camphor bound Cytochrome P450cam, Arg365Leu, Glu366Gln, monoclinic crystal form

spinqualitylabelsall models 3fwg, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fwg is a 2 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: CAM, HEM, K, TRS 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 The unique monooxygenase activity of cytochrome P450cam has been attributed to coordination of a cysteine thiolate to the heme cofactor. To investigate this interaction, we replaced cysteine with the more electron-donating selenocysteine. Good yields of the selenoenzyme were obtained by bacterial expression of an engineered gene containing the requisite UGA codon for selenocysteine and a simplified yet functional selenocysteine insertion sequence (SECIS). The sulfur-to-selenium substitution subtly modulates the structural, electronic, and catalytic properties of the enzyme. Catalytic activity decreases only 2-fold, whereas substrate oxidation becomes partially uncoupled from electron transfer, implying a more complex role for the axial ligand than generally assumed. Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine.,Aldag C, Gromov IA, Garcia-Rubio I, von Koenig K, Schlichting I, Jaun B, Hilvert D Proc Natl Acad Sci U S A. 2009 Mar 17. PMID:19293375 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

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