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'''CYTOCHROME P450CAM FROM PSEUDOMONAS PUTIDA, COMPLEXED WITH 1S-CAMPHOR''' | '''CYTOCHROME P450CAM FROM PSEUDOMONAS PUTIDA, COMPLEXED WITH 1S-CAMPHOR''' | ||
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[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Schulze, H.]] | [[Category: Schulze, H.]] | ||
[[Category: | [[Category: Cytochrome p450]] | ||
[[Category: | [[Category: Electron transport]] | ||
[[Category: | [[Category: Monooxygenase]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Oxygenase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:22:58 2008'' | |||
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Revision as of 07:22, 2 May 2008
CYTOCHROME P450CAM FROM PSEUDOMONAS PUTIDA, COMPLEXED WITH 1S-CAMPHOR
Overview
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.
About this Structure
1AKD is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer., Schlichting I, Jung C, Schulze H, FEBS Lett. 1997 Oct 6;415(3):253-7. PMID:9357977 Page seeded by OCA on Fri May 2 10:22:58 2008
