Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor 
enantiomer

Schlichting, Ilme; Jung, Christiane; Schulze, Heike

doi:10.1016/S0014-5793(97)01135-6

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Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer

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Schlichting, Ilme
Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Schlichting, I., Jung, C., & Schulze, H. (1997). Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer. FEBS Letters, 415(3), 253-257. doi:10.1016/S0014-5793(97)01135-6.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-A577-9

Abstract

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.