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[[Image:6cpp.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION==
|PDB= 6cpp |SIZE=350|CAPTION= <scene name='initialview01'>6cpp</scene>, resolution 1.9&Aring;
<StructureSection load='6cpp' size='340' side='right'caption='[[6cpp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>
<table><tr><td colspan='2'>[[6cpp]] 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=6CPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CPP FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAE:CAMPHANE'>CAE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpp OCA], [https://pdbe.org/6cpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cpp RCSB], [https://www.ebi.ac.uk/pdbsum/6cpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU] Involved in a camphor oxidation system.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/6cpp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=6cpp ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION'''
==See Also==
 
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
X-ray crystal structures have been determined for complexes of cytochrome P-450CAM with the substrates camphane, adamantane, and thiocamphor. Unlike the natural substrate camphor, which hydrogen bonds to Tyr96 and is metabolized to a single product, camphane, adamantane and thiocamphor do not hydrogen bond to the enzyme and all are hydroxylated at multiple positions. Evidently the lack of a substrate-enzyme hydrogen bond allows substrates greater mobility in the active site, explaining this lower regiospecificity of metabolism as well as the inability of these substrates to displace the distal ligand to the heme iron. Tyr96 is a ligand, via its carbonyl oxygen atom, to a cation that is thought to stabilize the camphor-P-450CAM complex [Poulos, T. L., Finzel, B. C., &amp; Howard, A. J. (1987) J. Mol. Biol. 195, 687-700]. The occupancy and temperature factor of the cationic site are lower and higher, respectively, in the presence of the non-hydrogen-bonding substrates investigated here than in the presence of camphor, underscoring the relationship between cation and substrate binding. Thiocamphor gave the most unexpected orientation in the active site of any of the substrates we have investigated to date. The orientation of thiocamphor is quite different from that of camphor. That is, carbons 5 and 6, at which thiocamphor is primarily hydroxylated [Atkins, W. M., &amp; Sligar, S. G. (1988) J. Biol. Chem. 263, 18842-18849], are positioned near Tyr96 rather than near the heme iron. Therefore, the crystallographically observed thiocamphor-P-450CAM structure may correspond to a nonproductive complex. Disordered solvent has been identified in the active site in the presence of uncoupling substrates that channel reducing equivalents away from substrate hydroxylation toward hydrogen peroxide and/or "excess" water production. A buried solvent molecule has also been identified, which may promote uncoupling by moving from an internal location to the active site in the presence of highly mobile substrates.
[[Category: Large Structures]]
 
==About this Structure==
6CPP 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=6CPP OCA].
 
==Reference==
Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation., Raag R, Poulos TL, Biochemistry. 1991 Mar 12;30(10):2674-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2001355 2001355]
[[Category: Camphor 5-monooxygenase]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Poulos TL]]
[[Category: Poulos, T L.]]
[[Category: Raag R]]
[[Category: Raag, R.]]
[[Category: CAE]]
[[Category: HEM]]
[[Category: oxidoreductase(oxygenase)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:13:19 2008''

Latest revision as of 17:29, 13 March 2024

CRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATIONCRYSTAL STRUCTURES OF CYTOCHROME P450-CAM COMPLEXED WITH CAMPHANE, THIOCAMPHOR, AND ADAMANTANE: FACTORS CONTROLLING P450 SUBSTRATE HYDROXYLATION

Structural highlights

6cpp is a 1 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CPXA_PSEPU Involved in a camphor oxidation system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

6cpp, resolution 1.90Å

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