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1akd

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==Overview==
==Overview==
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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.
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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==
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[[Category: oxygenase]]
[[Category: oxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:30:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:28 2008''

Revision as of 09:45, 21 February 2008

Image:1akd.gif

1akd, resolution 1.8Å

Drag the structure with the mouse to rotate

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 , and as ligands. Active as Camphor 5-monooxygenase, with EC number 1.14.15.1 Known structural/functional Sites: and . 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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