1akd: Difference between revisions
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==Overview== | ==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, . | 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== | ==About this Structure== | ||
1AKD is a | 1AKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with K, HEM and CAM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Structure known Active Sites: HEM and K. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AKD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: oxygenase]] | [[Category: oxygenase]] | ||
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Revision as of 11:58, 5 November 2007
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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 with K, HEM and CAM as ligands. Active as Camphor 5-monooxygenase, with EC number 1.14.15.1 Structure known Active Sites: HEM and K. 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
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