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[[Image:1akd.gif|left|200px]]
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{{STRUCTURE_1akd|  PDB=1akd  |  SCENE=  }}
'''CYTOCHROME P450CAM FROM PSEUDOMONAS PUTIDA, COMPLEXED WITH 1S-CAMPHOR'''


==CYTOCHROME P450CAM FROM PSEUDOMONAS PUTIDA, COMPLEXED WITH 1S-CAMPHOR==
<StructureSection load='1akd' size='340' side='right'caption='[[1akd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1akd]] 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=1AKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AKD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=1akd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akd OCA], [https://pdbe.org/1akd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1akd RCSB], [https://www.ebi.ac.uk/pdbsum/1akd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1akd 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/ak/1akd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1akd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:9357977</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1AKD 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=1AKD OCA].
</div>
<div class="pdbe-citations 1akd" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/9357977 9357977]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
[[Category: Camphor 5-monooxygenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Jung C]]
[[Category: Jung, C.]]
[[Category: Schlichting I]]
[[Category: Schlichting, I.]]
[[Category: Schulze H]]
[[Category: Schulze, H.]]
[[Category: Cytochrome p450]]
[[Category: Electron transport]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]
[[Category: Oxygenase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:22:58 2008''
Retrieved from "https://proteopedia.org/1akd"