Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.
The crystal structure of cytochrome P-450cam complexed with the enantiomer (1S)-camphor has been solved to 1.8 angstroms resolution and compared with the structure of the (1R)-camphor P-450cam complex. The overall protein structure is the same for both enantiomer complexes. However, the orientation of the substrates in the heme pocket differs. In contrast to (1R)-camphor, the (1S)-enantiomer binds in at least two orientations. The major binding mode of (1S)-camphor resembles the one of the (1R)-enantiomer in that there is a hydrogen bond between Tyr-96 and the quinone group of camphor, and the 10-methyl group points towards the I-helix. The binding differs in that C-5 is not at a position suitable for hydroxylation. In the other orientation (1S)-camphor is not hydrogen bonded, but C-5 is located suitably for hydroxylation.
Schlichting
I
I
Max Planck Institute for Molecular Physiology, Division for Physical Biochemistry, Dortmund, Germany.
Jung
C
C
Schulze
H
H
D002164:Camphor / Q000737:chemistry* / Q000378:metabolism; D019475:Camphor 5-Monooxygenase / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000737:chemistry / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D012984:Software; D013237:Stereoisomerism
D011994:Recombinant Proteins; D002164:Camphor; D019475:Camphor 5-Monooxygenase