2h7r | pdb_00002h7r

L244A mutant of Cytochrome P450cam complexed with imidazole

spinqualitylabelsall models 2h7r, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h7r 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: 1MZ, HEM Related: 1phc, 2cpp, 2h7q, 2h7s 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 We have identified a P450(cam) mutation, L244A, that mitigates the affinity for imidazole and substituted imidazoles while maintaining a high affinity for the natural substrate camphor. The P450(cam) L244A crystal structure solved in the absence of any ligand reveals that the I-helix is displaced inwards by over 1 A in response to the cavity created by the change from leucine to alanine. Furthermore, the crystal structures of imidazole-bound P450(cam) and the 1-methylimidazole-bound P450(cam) L244A mutant reveal that the ligands have distinct binding modes in the two proteins. Whereas in wild-type P450(cam) the imidazole coordinates to the iron in an orientation roughly perpendicular to the plane of the heme, in the L244A mutant the rearranged I helix, and specifically residue Val247, forces the imidazole into an orientation almost parallel to the heme that impairs its ability to coordinate to the heme iron. As a result, the imidazole is much more weakly bound to the mutant than it is to the wild-type enzyme. Despite the constriction of the active site by the mutation, previous work with the L244A mutant has shown that it oxidizes larger substrates than the wild-type enzyme. This paradoxical situation, in which a mutation that nominally increases the active site cavity appears to decrease it, suggests that the mutation actually increases the active site maleability, allowing it to better expand to oxidize larger substrates. Cytochrome P450 active site plasticity: attenuation of imidazole binding in cytochrome P450(cam) by an L244A mutation.,Verras A, Alian A, de Montellano PR Protein Eng Des Sel. 2006 Nov;19(11):491-6. Epub 2006 Aug 30. PMID:16943206 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

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