1geb: Difference between revisions

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-[[Image:1geb.png|left|200px]]
-{{STRUCTURE_1geb|  PDB=1geb  |  SCENE=  }}
+==X-RAY CRYSTAL STRUCTURE AND CATALYTIC PROPERTIES OF THR252ILE MUTANT OF CYTOCHROME P450CAM==
+<StructureSection load='1geb' size='340' side='right'caption='[[1geb]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1geb]] 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=1GEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GEB 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]] 2.03&#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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1geb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1geb OCA], [https://pdbe.org/1geb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1geb RCSB], [https://www.ebi.ac.uk/pdbsum/1geb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1geb 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/ge/1geb_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=1geb ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structure-function relationship in cytochrome P450cam monooxygenase was studied by employing its active site mutant Thr252Ile. X-ray crystallographic analyses of the ferric d-camphor-bound form of the mutant revealed that the mutation caused a structural change in the active site giving an enlarged oxygen-binding pocket that did not contain any hydrophilic group such as the OH group of Thr and H(2)O. The enzyme showed a low monooxygenase activity of ca. 1/10 of the activity of the wild-type enzyme. Kinetic analyses of each catalytic step revealed that the rate of proton-coupled reduction of the oxygenated intermediate of the enzyme, a ternary complex of dioxygen and d-camphor with the ferrous enzyme, decreased to about 1/30 of that of the wild-type enzyme, while the rates of other catalytic steps including the reduction of the ferric d-camphor-bound form by reduced putidaredoxin did not change significantly. These results indicated that a hydrophilic group(s) such as water and/or hydroxyl group in the active site is prerequisite to a proton supply for the reduction of the oxygenated intermediate, thereby giving support for the operation of a proton transfer network composed of Thr252, Asp251, and two other amino acids and water proposed by previous investigators.
-===X-RAY CRYSTAL STRUCTURE AND CATALYTIC PROPERTIES OF THR252ILE MUTANT OF CYTOCHROME P450CAM===
+X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center.,Hishiki T, Shimada H, Nagano S, Egawa T, Kanamori Y, Makino R, Park SY, Adachi S, Shiro Y, Ishimura Y J Biochem. 2000 Dec;128(6):965-74. PMID:11098139<ref>PMID:11098139</ref>
-{{ABSTRACT_PUBMED_11098139}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1geb" style="background-color:#fffaf0;"></div>
-[[1geb]] is a 1 chain structure of [[Cytochrome P450]] with 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=1GEB OCA].
 ==See Also==
-*[[Cytochrome P450|Cytochrome P450]]
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011098139</ref><references group="xtra"/>
+__TOC__
-[[Category: Camphor 5-monooxygenase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Pseudomonas putida]]
-[[Category: Hishiki, T.]]
+[[Category: Hishiki T]]
-[[Category: Ishimura, Y.]]
+[[Category: Ishimura Y]]
-[[Category: Nagano, S.]]
+[[Category: Nagano S]]
-[[Category: Park, S Y.]]
+[[Category: Park S-Y]]
-[[Category: Shimada, H.]]
+[[Category: Shimada H]]
-[[Category: Cytochrome p450cam]]
-[[Category: Electron transport]]
-[[Category: Monooxygenase]]