2fe6

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[[Image:2fe6.gif|left|200px]]
 
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==P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX==
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The line below this paragraph, containing "STRUCTURE_2fe6", creates the "Structure Box" on the page.
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<StructureSection load='2fe6' size='340' side='right'caption='[[2fe6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2fe6]] 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=2FE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FE6 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.5&#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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MNR:PROTOPORPHYRIN+IX+CONTAINING+MN'>MNR</scene></td></tr>
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{{STRUCTURE_2fe6| PDB=2fe6 | SCENE= }}
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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=2fe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fe6 OCA], [https://pdbe.org/2fe6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fe6 RCSB], [https://www.ebi.ac.uk/pdbsum/2fe6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fe6 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/fe/2fe6_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=2fe6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.
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'''P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX'''
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The status of high-valent metal oxo complexes in the P450 cytochromes.,Makris TM, von Koenig K, Schlichting I, Sligar SG J Inorg Biochem. 2006 Apr;100(4):507-18. Epub 2006 Feb 28. PMID:16510191<ref>PMID:16510191</ref>
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==Overview==
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The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2FE6 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=2FE6 OCA].
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</div>
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<div class="pdbe-citations 2fe6" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The status of high-valent metal oxo complexes in the P450 cytochromes., Makris TM, von Koenig K, Schlichting I, Sligar SG, J Inorg Biochem. 2006 Apr;100(4):507-18. Epub 2006 Feb 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16510191 16510191]
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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[[Category: Camphor 5-monooxygenase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Makris TM]]
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[[Category: Koenig, K von.]]
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[[Category: Schlichting I]]
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[[Category: Makris, T M.]]
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[[Category: Sligar SG]]
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[[Category: Schlichting, I.]]
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[[Category: Von Koenig K]]
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[[Category: Sligar, S G.]]
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[[Category: Heme]]
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[[Category: Manganic]]
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[[Category: Mono-oxygenase]]
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[[Category: Substrate-free]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:47:21 2008''
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Current revision

P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX

PDB ID 2fe6

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