1dz8: Difference between revisions

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-[[Image:1dz8.jpg|left|200px]]
- {{Structure
+==oxygen complex of p450cam from pseudomonas putida==
-|PDB= 1dz8 |SIZE=350|CAPTION= <scene name='initialview01'>1dz8</scene>, resolution 1.9&Aring;
+<StructureSection load='1dz8' size='340' side='right'caption='[[1dz8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE= <scene name='pdbsite=K1:This+Is+The+Intramolecular+K+Binding+Site+For+Monomer+A+...'>K1</scene>, <scene name='pdbsite=K2:This+Is+The+Intramolecular+K+Binding+Site+For+Monomer+B+...'>K2</scene>, <scene name='pdbsite=K3:Intermolecular+K+Site'>K3</scene> and <scene name='pdbsite=O2:O'>O2</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
+<table><tr><td colspan='2'>[[1dz8]] is a 2 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=1DZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZ8 FirstGlance]. <br>
-|ACTIVITY=
+</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=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=1dz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz8 OCA], [https://pdbe.org/1dz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dz8 RCSB], [https://www.ebi.ac.uk/pdbsum/1dz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz8 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/dz/1dz8_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=1dz8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.
-'''OXYGEN COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA'''
+The catalytic pathway of cytochrome p450cam at atomic resolution.,Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG Science. 2000 Mar 3;287(5458):1615-22. PMID:10698731<ref>PMID:10698731</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1dz8" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-DZ8 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=1DZ8 OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-The catalytic pathway of cytochrome p450cam at atomic resolution., Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG, Science. 2000 Mar 3;287(5458):1615-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10698731 10698731]
 [[Category: Pseudomonas putida]]
-[[Category: Single protein]]
+[[Category: Benson DE]]
-[[Category: Benson, D E.]]
+[[Category: Berendzen J]]
-[[Category: Berendzen, J.]]
+[[Category: Chu K]]
-[[Category: Chu, K.]]
+[[Category: Maves SA]]
-[[Category: Maves, S A.]]
+[[Category: Petsko GA]]
-[[Category: Petsko, G A.]]
+[[Category: Ringe D]]
-[[Category: Ringe, D.]]
+[[Category: Schlichting I]]
-[[Category: Schlichting, I.]]
+[[Category: Sligar SG]]
-[[Category: Sligar, S G.]]
+[[Category: Stock AM]]
-[[Category: Stock, A M.]]
+[[Category: Sweet RM]]
-[[Category: Sweet, R M.]]
-[[Category: CAM]]
-[[Category: HEM]]
-[[Category: K]]
-[[Category: OXY]]
-[[Category: TRS]]
-[[Category: heme]]
-[[Category: mono-oxygenase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:46:51 2008''