2zaw

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(New page: 200px<br /><applet load="2zaw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2zaw, resolution 1.55&Aring;" /> '''Crystal Structure of...)
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[[Image:2zaw.jpg|left|200px]]<br /><applet load="2zaw" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2zaw, resolution 1.55&Aring;" />
 
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'''Crystal Structure of Ferric Cytochrome P450cam Reconstituted with 6-Methyl-6-depropionated Hemin'''<br />
 
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==Overview==
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==Crystal Structure of Ferric Cytochrome P450cam Reconstituted with 6-Methyl-6-depropionated Hemin==
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Cytochrome P450cam (P450cam) binds a protoheme IX as a prosthetic group, via noncovalent interactions. Heme-6-propionate, one of the two, heme-propionate side chains, forms hydrogen-bonding interactions with, Arg112 and other hydrophilic amino acid residues. Here, we demonstrate the, structural and functional roles of the 6-propionate side chain in P450cam, using a reconstituted protein with 6-depropionate-6-methylated protoheme, IX (one-legged heme). The spectroscopic data and the enzymatic activities, reveal that removal of the 6-propionate has no clear influence on the, enzyme property. The rate of electron transfer from putidaredoxin (Pdx), a, natural redox partner, to P450cam was not significantly changed, whereas, the removal of the 6-propionate decreased the affinity of Pdx by 3.5-fold, supporting the proposed role of Arg112 as the essential constituent of the, Pdx binding site. Resonance Raman experiments indicate that removal of the, 6-propionate weakens the Fe-S bond strength. The X-ray structure of the, reconstituted protein at 1.55 A resolution is highly superimposable with, that of the wild-type protein, whereas the thiolate of the Cys357 heme, ligand in the reconstituted protein is visible from the protein surface, owing to the lack of the 6-propionate. Lengthening of the Fe-S bond and, the water accessibility could facilitate protonation of thiolate anion to, thiol, explaining the observed formation of the inactive P420 species, under the mild conditions. Therefore, the d-camphor hydroxylation reaction, requires a 6-propionate-protein matrix interaction to maintain an active, P450 species.
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<StructureSection load='2zaw' size='340' side='right'caption='[[2zaw]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2zaw]] 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=2ZAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZAW FirstGlance]. <br>
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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]] 1.55&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6HE:6-METHY-6-DEPROPIONATEHEMIN'>6HE</scene>, <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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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=2zaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zaw OCA], [https://pdbe.org/2zaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zaw RCSB], [https://www.ebi.ac.uk/pdbsum/2zaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zaw 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/za/2zaw_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=2zaw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2ZAW 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 <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=6HE:'>6HE</scene> and <scene name='pdbligand=CAM:'>CAM</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAW OCA].
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Evaluation of the Functional Role of the Heme-6-propionate Side Chain in Cytochrome P450cam., Harada K, Sakurai K, Ikemura K, Ogura T, Hirota S, Shimada H, Hayashi T, J Am Chem Soc. 2007 Dec 19;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18088124 18088124]
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[[Category: Large Structures]]
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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: Harada K]]
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[[Category: Harada, K.]]
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[[Category: Hayashi T]]
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[[Category: Hayashi, T.]]
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[[Category: Sakurai K]]
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[[Category: Sakurai, K.]]
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[[Category: Shimada H]]
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[[Category: Shimada, H.]]
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[[Category: Tsukihara T]]
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[[Category: Tsukihara, T.]]
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[[Category: 6HE]]
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[[Category: CAM]]
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[[Category: CL]]
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[[Category: K]]
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[[Category: camphor-hydroxylase]]
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[[Category: heme]]
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[[Category: iron]]
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[[Category: membrane]]
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[[Category: metal-binding]]
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[[Category: monooxygenase]]
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[[Category: oxidoreductase]]
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[[Category: p450cam]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:46:59 2008''
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Current revision

Crystal Structure of Ferric Cytochrome P450cam Reconstituted with 6-Methyl-6-depropionated Hemin

PDB ID 2zaw

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