2cpp
From Proteopedia
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[[Image:2cpp.gif|left|200px]] | [[Image:2cpp.gif|left|200px]] | ||
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'''HIGH-RESOLUTION CRYSTAL STRUCTURE OF CYTOCHROME P450-CAM''' | '''HIGH-RESOLUTION CRYSTAL STRUCTURE OF CYTOCHROME P450-CAM''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CPP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. This structure supersedes the now removed PDB entry | + | 2CPP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cpp 1cpp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CPP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
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Revision as of 19:45, 3 May 2008
HIGH-RESOLUTION CRYSTAL STRUCTURE OF CYTOCHROME P450-CAM
Overview
The crystal structure of Pseudomonas putida cytochrome P450cam with its substrate, camphor, bound has been refined to R = 0.19 at a normal resolution of 1.63 A. While the 1.63 A model confirms our initial analysis based on the 2.6 A model, the higher resolution structure has revealed important new details. These include a more precise assignment of sequence to secondary structure, the identification of three cis-proline residues, and a more detailed picture of substrate-protein interactions. In addition, 204 ordered solvent molecules have been found, one of which appears to be a cation. The cation stabilizes an unfavorable polypeptide conformation involved in forming part of the active site pocket, suggesting that the cation may be the metal ion binding site associated with the well-known ability of metal ions to enhance formation of the enzyme-substrate complex. Another unusual polypeptide conformation forms the proposed oxygen-binding pocket. A localized distortion and widening of the distal helix provides a pocket for molecular oxygen. An intricate system of side-chain to backbone hydrogen bonds aids in stabilizing the required local disruption in helical geometry. Sequence homologies strongly suggest a common oxygen-binding pocket in all P450 species. Further sequence comparisons between P450 species indicate common three-dimensional structures with changes focused in a region of the molecule postulated to be associated with the control of substrate specificity.
About this Structure
2CPP is a Single protein structure of sequence from Pseudomonas putida. This structure supersedes the now removed PDB entry 1cpp. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structure of cytochrome P450cam., Poulos TL, Finzel BC, Howard AJ, J Mol Biol. 1987 Jun 5;195(3):687-700. PMID:3656428 Page seeded by OCA on Sat May 3 22:45:07 2008
