2L8M

Reduced and CO-bound cytochrome P450cam (CYP101A1)

Summary for 2L8M

• Entry DOI: 10.2210/pdb2l8m/pdb
• Related: 3CPP
• Descriptor: Camphor 5-monooxygenase, CAMPHOR, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total)
• Functional Keywords: metalloenzyme, monooxygenase, oxidoreductase
• Biological source: Pseudomonas putida
• Cellular location: Cytoplasm (By similarity): P00183
• Total number of polymer chains: 1
• Total formula weight: 47779.56

Authors

Pochapsky, T.C.,Pochapsky, S.S.,Dang, M.,Asciutto, E.,Madura, J. (deposition date: 2011-01-19, release date: 2011-02-16, Last modification date: 2024-05-15)

Primary citation

Asciutto, E.K.,Dang, M.,Pochapsky, S.S.,Madura, J.D.,Pochapsky, T.C.
Experimentally Restrained Molecular Dynamics Simulations for Characterizing the Open States of Cytochrome P450(cam).
Biochemistry, 50:1664-1671, 2011

PubMed Abstract: 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.

PubMed: 21265500
DOI: 10.1021/bi101820d

Experimental method

SOLUTION NMR