View source for 5cpp

[[Image:5cpp.gif|left|200px]]<br /><applet load="5cpp" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="5cpp, resolution 2.08&Aring;" />
'''THE STRUCTURAL BASIS FOR SUBSTRATE-INDUCED CHANGES IN REDOX POTENTIAL AND SPIN EQUILIBRIUM IN CYTOCHROME P-450(CAM)'''<br />

==Overview==
The crystal structures of cytochrome P-450CAM complexed with the, alternative substrates norcamphor and adamantanone have been refined at, 2.0-A resolution and compared with the native, camphor-bound form of the, enzyme. Norcamphor lacks the 8-, 9-, and 10-methyl groups of camphor., Thus, specific interactions between these groups and phenylalanine 87 and, valines 247 and 295 are missing in the norcamphor complex. As a result, norcamphor binds about 0.9 A further from the oxygen-binding site than, does camphor, which allows sufficient room for a water molecule or, hydroxide ion to remain coordinated with the heme iron atom. The larger, adamantanone occupies a position closer to that of camphor and, as in the, camphor-bound enzyme, the heme iron remains pentacoordinate with no, solvent molecule coordinated as a sixth ligand. A comparison of, crystallographic temperature factors indicates that norcamphor is more, "loosely" bound than are either camphor or adamantanone, as might be, expected from the relative sizes of the different substrates. The looser, fit of norcamphor in the active-site pocket results in a less specific, pattern of hydroxylation. The presence of an aqua ligand is the likely, structural basis for the norcamphor-P-450CAM complex having both a lower, redox potential and higher percentage of low-spin heme than do either the, camphor-P-450CAM or adamantanone-P-450CAM complexes.

==About this Structure==
5CPP 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 HEM and ADO 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5CPP OCA]. 

==Reference==
The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM., Raag R, Poulos TL, Biochemistry. 1989 Jan 24;28(2):917-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2713354 2713354]
[[Category: Camphor 5-monooxygenase]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Poulos, T.L.]]
[[Category: Raag, R.]]
[[Category: ADO]]
[[Category: HEM]]
[[Category: oxidoreductase(oxygenase)]]

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