1p2y

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[[Image:1p2y.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF CYTOCHROME P450CAM IN COMPLEX WITH (S)-(-)-NICOTINE==
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The line below this paragraph, containing "STRUCTURE_1p2y", creates the "Structure Box" on the page.
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<StructureSection load='1p2y' size='340' side='right'caption='[[1p2y]], [[Resolution|resolution]] 2.30&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'>[[1p2y]] 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=1P2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P2Y 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]] 2.3&#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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NCT:(S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE'>NCT</scene></td></tr>
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{{STRUCTURE_1p2y| PDB=1p2y | 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=1p2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2y OCA], [https://pdbe.org/1p2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p2y RCSB], [https://www.ebi.ac.uk/pdbsum/1p2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2y 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/p2/1p2y_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=1p2y ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF CYTOCHROME P450CAM IN COMPLEX WITH (S)-(-)-NICOTINE'''
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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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Crystallographic and spectroscopic studies have been undertaken to characterize the binding behavior of the non-native substrate nicotine in the active site of the monooxygenase hemoprotein cytochrome P450cam. Despite the existence of a theoretical model that is consistent with the observed distribution of monooxygenation products, the crystal structure of the complex indicates that the primary binding mode of nicotine is unproductive. The structure is confirmed by spectral data that indicate direct coordination of substrate pyridine nitrogen with the heme iron. This would be the proper structure for evaluating binding affinity and inhibition. Reduction of the heme from Fe(III) to Fe(II) and introduction of carbon monoxide into crystals of the nicotine-P450cam complex, to simulate molecular oxygen binding, produces reorientation of the nicotine. This orientation is the appropriate one for predicting regioselectivity and the kinetic features of substrate oxidation. While it is not clear that such complicated behavior will be exhibited for other enzyme-substrate interactions, it is clear that a single crystal structure for a given substrate-enzyme interaction may not provide a good description of the binding mode responsible for product formation.
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[[Category: Large Structures]]
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==About this Structure==
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1P2Y 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=1P2Y OCA].
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==Reference==
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Crystallographic studies on the complex behavior of nicotine binding to P450cam (CYP101)., Strickler M, Goldstein BM, Maxfield K, Shireman L, Kim G, Matteson DS, Jones JP, Biochemistry. 2003 Oct 21;42(41):11943-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14556625 14556625]
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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: Goldstein BM]]
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[[Category: Goldstein, B M.]]
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[[Category: Jones JP]]
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[[Category: Jones, J P.]]
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[[Category: Kim G]]
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[[Category: Kim, G.]]
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[[Category: Matteson D]]
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[[Category: Matteson, D.]]
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[[Category: Maxfield K]]
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[[Category: Maxfield, K.]]
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[[Category: Shireman L]]
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[[Category: Shireman, L.]]
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[[Category: Strickler M]]
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[[Category: Strickler, M.]]
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[[Category: Heme]]
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[[Category: Monooxygenase]]
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[[Category: Nicotine]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:36:59 2008''
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Current revision

CRYSTAL STRUCTURE OF CYTOCHROME P450CAM IN COMPLEX WITH (S)-(-)-NICOTINE

PDB ID 1p2y

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