1ebe

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[[Image:1ebe.png|left|200px]]
 
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==Laue diffraction study on the structure of cytochrome c peroxidase compound I==
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The line below this paragraph, containing "STRUCTURE_1ebe", creates the "Structure Box" on the page.
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<StructureSection load='1ebe' size='340' side='right'caption='[[1ebe]], [[Resolution|resolution]] 2.20&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'>[[1ebe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EBE 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]] 2.2&#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=O:OXYGEN+ATOM'>O</scene></td></tr>
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{{STRUCTURE_1ebe| PDB=1ebe | 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=1ebe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebe OCA], [https://pdbe.org/1ebe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ebe RCSB], [https://www.ebi.ac.uk/pdbsum/1ebe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ebe ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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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/eb/1ebe_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=1ebe 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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BACKGROUND: Cytochrome c peroxidase from yeast is a soluble haem-containing protein found in the mitochondrial electron transport chain where it probably protects against toxic peroxides. The aim of this study was to obtain a reliable structure for the doubly oxidized transient intermediate (termed compound I) in the reaction of cytochrome c peroxidase with hydrogen peroxide. This intermediate contains a semistable free radical on Trp191, and an oxyferryl haem group. RESULTS: Compound I was produced in crystals of yeast cytochrome c peroxidase by reacting the crystalline enzyme with hydrogen peroxide in a flow cell. The reaction was monitored by microspectrophotometry and Laue crystallography in separate experiments. A nearly complete conversion to compound I was achieved within two minutes of the addition of hydrogen peroxide, and the concentration of the intermediate remained at similar levels for an additional half an hour. The structure of the intermediate was determined by Laue diffraction. The refined Laue structure for compound I shows clear structural changes at the peroxide-binding site but no significant changes at the radical site. The photographs were processed with a new software package (LEAP), overcoming many of the former problems encountered in extracting structural information from Laue exposures. CONCLUSIONS: The geometry of the haem environment in this protein allows structural changes to be extremely small, similar in magnitude to those observed for the Fe2+/Fe3+ transition in cytochrome c. The results suggest that these molecules have evolved to transfer electrons with a minimal need for structural adjustment.
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===LAUE DIFFRACTION STUDY ON THE STRUCTURE OF CYTOCHROME C PEROXIDASE COMPOUND I===
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Laue diffraction study on the structure of cytochrome c peroxidase compound I.,Fulop V, Phizackerley RP, Soltis SM, Clifton IJ, Wakatsuki S, Erman J, Hajdu J, Edwards SL Structure. 1994 Mar 15;2(3):201-8. PMID:8069633<ref>PMID:8069633</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ebe" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8069633}}, adds the Publication Abstract to the page
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8069633 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8069633}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1ebe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBE OCA].
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==Reference==
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<ref group="xtra">PMID:8069633</ref><ref group="xtra">PMID:6092361</ref><references group="xtra"/>
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[[Category: Cytochrome-c peroxidase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Clifton, I J.]]
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[[Category: Clifton IJ]]
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[[Category: Edwards, S L.]]
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[[Category: Edwards SL]]
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[[Category: Erman, J E.]]
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[[Category: Erman JE]]
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[[Category: Fulop, V.]]
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[[Category: Fulop V]]
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[[Category: Hajdu, J.]]
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[[Category: Hajdu J]]
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[[Category: Phizackerley, R P.]]
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[[Category: Phizackerley RP]]
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[[Category: Soltis, S M.]]
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[[Category: Soltis SM]]
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[[Category: Wakatsuki, S.]]
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[[Category: Wakatsuki S]]
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[[Category: Compound i]]
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[[Category: Laue diffraction]]
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[[Category: Oxidoreductase]]
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Current revision

Laue diffraction study on the structure of cytochrome c peroxidase compound I

PDB ID 1ebe

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Proteopedia Page Contributors and Editors (what is this?)

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