2qbm: Difference between revisions

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OCA

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-[[Image:2qbm.jpg|left|200px]]<br /><applet load="2qbm" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2qbm, resolution 1.80&Aring;" />
-'''Crystal structure of the P450cam G248T mutant in the cyanide bound state'''<br />
-==Overview==
+==Crystal structure of the P450cam G248T mutant in the cyanide bound state==
-Distal pocket water molecules have been widely implicated in the delivery, of protons required in O-O bond heterolysis in the P450 reaction cycle., Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket, through mutagenesis of a distal pocket glycine to either valine or, threonine results in the alteration of spin state equilibria, and has, dramatic consequences on the catalytic rate, coupling efficiency, and, kinetic solvent isotope effect parameters, highlighting an important role, of the active-site hydration level on P450 catalysis. Cryoradiolysis of, the mutant CYP101 oxyferrous complexes further indicates a specific, perturbation of proton-transfer events required for the transformation of, ferric-peroxo to ferric-hydroperoxo states. Finally, crystallography of, the 248Val and 248Thr mutants in both the ferric camphor bound resting, state and ferric-cyano adducts shows both the alteration of, hydrogen-bonding networks and the alteration of heme geometry parameters., Taken together, these results indicate that the distal pocket, microenvironment governs the transformation of reactive heme-oxygen, intermediates in P450 cytochromes.
+<StructureSection load='2qbm' size='340' side='right'caption='[[2qbm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2qbm]] 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=2QBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QBM 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=CYN:CYANIDE+ION'>CYN</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=2qbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qbm OCA], [https://pdbe.org/2qbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qbm RCSB], [https://www.ebi.ac.uk/pdbsum/2qbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qbm 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/qb/2qbm_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=2qbm ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Distal pocket water molecules have been widely implicated in the delivery of protons required in O-O bond heterolysis in the P450 reaction cycle. Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket through mutagenesis of a distal pocket glycine to either valine or threonine results in the alteration of spin state equilibria, and has dramatic consequences on the catalytic rate, coupling efficiency, and kinetic solvent isotope effect parameters, highlighting an important role of the active-site hydration level on P450 catalysis. Cryoradiolysis of the mutant CYP101 oxyferrous complexes further indicates a specific perturbation of proton-transfer events required for the transformation of ferric-peroxo to ferric-hydroperoxo states. Finally, crystallography of the 248Val and 248Thr mutants in both the ferric camphor bound resting state and ferric-cyano adducts shows both the alteration of hydrogen-bonding networks and the alteration of heme geometry parameters. Taken together, these results indicate that the distal pocket microenvironment governs the transformation of reactive heme-oxygen intermediates in P450 cytochromes.
-==About this Structure==
+Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry.,Makris TM, von Koenig K, Schlichting I, Sligar SG Biochemistry. 2007 Dec 11;46(49):14129-40. Epub 2007 Nov 15. PMID:18001135<ref>PMID:18001135</ref>
-QBM 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=CYN:'>CYN</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=HEM:'>HEM</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=2QBM OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Alteration of P450 Distal Pocket Solvent Leads to Impaired Proton Delivery and Changes in Heme Geometry., Makris TM, Koenig KV, Schlichting I, Sligar SG, Biochemistry. 2007 Dec 11;46(49):14129-14140. Epub 2007 Nov 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18001135 18001135]
+</div>
-[[Category: Camphor 5-monooxygenase]]
+<div class="pdbe-citations 2qbm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Pseudomonas putida]]
-[[Category: Single protein]]
+[[Category: Makris TM]]
-[[Category: Koenig, K.von.]]
+[[Category: Schlichting I]]
-[[Category: Makris, T.M.]]
+[[Category: Sligar SD]]
-[[Category: Schlichting, I.]]
+[[Category: Von Koenig K]]
-[[Category: Sligar, S.D.]]
-[[Category: CAM]]
-[[Category: CYN]]
-[[Category: HEM]]
-[[Category: K]]
-[[Category: conserved active site residue]]
-[[Category: cyanide complex]]
-[[Category: cyp101]]
-[[Category: gly248]]
-[[Category: heme geometry]]
-[[Category: mutant]]
-[[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:27:17 2008''