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[[Image:1zby.gif|left|200px]]
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{{STRUCTURE_1zby|  PDB=1zby  |  SCENE=  }}
'''High-Resolution Crystal Structure of Native (Resting) Cytochrome c Peroxidase (CcP)'''


==High-Resolution Crystal Structure of Native (Resting) Cytochrome c Peroxidase (CcP)==
<StructureSection load='1zby' size='340' side='right'caption='[[1zby]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zby]] 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=1ZBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZBY 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]] 1.2&#8491;</td></tr>
<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></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=1zby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zby OCA], [https://pdbe.org/1zby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zby RCSB], [https://www.ebi.ac.uk/pdbsum/1zby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zby ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== 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/zb/1zby_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1zby ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1). In addition, crystals were analyzed by UV-vis absorption and electron paramagnetic resonance spectroscopies before and after data collection to determine the state of the Fe(IV) center and the cationic Trp191 radical formed in Compound I. The results show that X-ray exposure does not lead to reduction of Fe(IV) and only partial reduction of the Trp radical. A comparison of the two structures reveals subtle but important conformational changes that aid in the stabilization of the Trp191 cationic radical in Compound I. The higher-resolution data also enable a more accurate determination of changes in heme parameters. Most importantly, when one goes from resting state Fe(III) to Compound I, the His-Fe bond distance increases, the iron moves into the porphyrin plane leading to shorter pyrrole N-Fe bonds, and the Fe(IV)-O bond distance is 1.87 A, suggesting a single Fe(IV)-O bond and not the generally accepted double bond.


==Overview==
High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.,Bonagura CA, Bhaskar B, Shimizu H, Li H, Sundaramoorthy M, McRee DE, Goodin DB, Poulos TL Biochemistry. 2003 May 20;42(19):5600-8. PMID:12741816<ref>PMID:12741816</ref>
Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1). In addition, crystals were analyzed by UV-vis absorption and electron paramagnetic resonance spectroscopies before and after data collection to determine the state of the Fe(IV) center and the cationic Trp191 radical formed in Compound I. The results show that X-ray exposure does not lead to reduction of Fe(IV) and only partial reduction of the Trp radical. A comparison of the two structures reveals subtle but important conformational changes that aid in the stabilization of the Trp191 cationic radical in Compound I. The higher-resolution data also enable a more accurate determination of changes in heme parameters. Most importantly, when one goes from resting state Fe(III) to Compound I, the His-Fe bond distance increases, the iron moves into the porphyrin plane leading to shorter pyrrole N-Fe bonds, and the Fe(IV)-O bond distance is 1.87 A, suggesting a single Fe(IV)-O bond and not the generally accepted double bond.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1ZBY is a [[Single protein]] structure of 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=1ZBY OCA].
</div>
<div class="pdbe-citations 1zby" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase., Bonagura CA, Bhaskar B, Shimizu H, Li H, Sundaramoorthy M, McRee DE, Goodin DB, Poulos TL, Biochemistry. 2003 May 20;42(19):5600-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12741816 12741816]
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
[[Category: Cytochrome-c peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Bhaskar B]]
[[Category: Bhaskar, B.]]
[[Category: Bonagura CA]]
[[Category: Bonagura, C A.]]
[[Category: Goodin DB]]
[[Category: Goodin, D B.]]
[[Category: Li H]]
[[Category: Li, H.]]
[[Category: McRee DE]]
[[Category: McRee, D E.]]
[[Category: Poulos TL]]
[[Category: Poulos, T L.]]
[[Category: Shimizu H]]
[[Category: Shimizu, H.]]
[[Category: Sundaramoorthy M]]
[[Category: Sundaramoorthy, M.]]
[[Category: Ccp]]
[[Category: Heme peroxidase]]
[[Category: High-spin heme]]
[[Category: Resting state]]
[[Category: Trp-cation radical]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:26:24 2008''
Retrieved from "https://proteopedia.org/1zby"