2l8m | pdb_00002l8m

Reduced and CO-bound cytochrome P450cam (CYP101A1)

spinqualitylabelsall models 2l8m Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l8m is a 1 chain structure with sequence from Pseudomonas putida. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: CAM, CL, CMO, HEM, K Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CPXA_PSEPU Involved in a camphor oxidation system. Publication Abstract from PubMed Residual dipolar couplings (RDCs) were used as restraints in fully solvated molecular dynamics simulations of reduced substrate- and carbonmonoxy-bound cytochrome P450(cam) (CYP101A1), a 414-residue soluble monomeric heme-containing camphor monooxygenase from the soil bacterium Pseudomonas putida. The (1)D(NH) residual dipolar couplings used as restraints were measured in two independent alignment media. A soft annealing protocol was used to heat the starting structures while incorporating the RDC restraints. After production dynamics, structures with the lowest total violation energies for RDC restraints were extracted to identify ensembles of conformers accessible to the enzyme in solution. The simulations result in substrate orientations different from that seen in crystallographic structures and a more open and accessible enzyme active site and largely support previously reported differences between the open and closed states of CYP101A1. Experimentally Restrained Molecular Dynamics Simulations for Characterizing the Open States of Cytochrome P450(cam).,Asciutto EK, Dang M, Pochapsky SS, Madura JD, Pochapsky TC Biochemistry. 2011 Feb 8. PMID:21265500 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

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