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7cpp

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[[Image:7cpp.gif|left|200px]]
 
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{{Structure
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==THE STRUCTURAL BASIS FOR SUBSTRATE-INDUCED CHANGES IN REDOX POTENTIAL AND SPIN EQUILIBRIUM IN CYTOCHROME P450(CAM)==
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|PDB= 7cpp |SIZE=350|CAPTION= <scene name='initialview01'>7cpp</scene>, resolution 2.0&Aring;
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<StructureSection load='7cpp' size='340' side='right'caption='[[7cpp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=NCM:NORCAMPHOR'>NCM</scene>
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<table><tr><td colspan='2'>[[7cpp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CPP FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NCM:NORCAMPHOR'>NCM</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cpp OCA], [https://pdbe.org/7cpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cpp RCSB], [https://www.ebi.ac.uk/pdbsum/7cpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cpp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU] Involved in a camphor oxidation system.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/7cpp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=7cpp ConSurf].
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<div style="clear:both"></div>
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'''THE STRUCTURAL BASIS FOR SUBSTRATE-INDUCED CHANGES IN REDOX POTENTIAL AND SPIN EQUILIBRIUM IN CYTOCHROME P450(CAM)'''
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==See Also==
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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7CPP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CPP OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/2713354 2713354]
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[[Category: Camphor 5-monooxygenase]]
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Poulos TL]]
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[[Category: Poulos, T L.]]
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[[Category: Raag R]]
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[[Category: Raag, R.]]
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[[Category: HEM]]
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[[Category: NCM]]
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[[Category: oxidoreductase(oxygenase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:14:23 2008''
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Current revision

THE STRUCTURAL BASIS FOR SUBSTRATE-INDUCED CHANGES IN REDOX POTENTIAL AND SPIN EQUILIBRIUM IN CYTOCHROME P450(CAM)

PDB ID 7cpp

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