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New page: left|200px<br /> <applet load="1oco" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oco, resolution 2.8Å" /> '''BOVINE HEART CYTOCHR...
 
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[[Image:1oco.gif|left|200px]]<br />
<applet load="1oco" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1oco, resolution 2.8&Aring;" />
'''BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE'''<br />


==Overview==
==BOVINE HEART CYTOCHROME C OXIDASE IN CARBON MONOXIDE-BOUND STATE==
Crystal structures of bovine heart cytochrome c oxidase in the fully, oxidized, fully reduced, azide-bound, and carbon monoxide-bound states, were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site, exchanges its effective accessibility to the matrix aqueous phase for one, to the cytosolic phase concomitantly with a significant decrease in the pK, of its carboxyl group, on reduction of the metal sites. The movement, indicates the aspartate as the proton pumping site. A tyrosine acidified, by a covalently linked imidazole nitrogen is a possible proton donor for, the O2 reduction by the enzyme.
<StructureSection load='1oco' size='340' side='right'caption='[[1oco]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oco]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The May 2000 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Cytochrome c Oxidase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2000_5 10.2210/rcsb_pdb/mom_2000_5]. The December 2002 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Cytochrome c''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2002_12 10.2210/rcsb_pdb/mom_2002_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OCO 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1oco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oco OCA], [https://pdbe.org/1oco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oco RCSB], [https://www.ebi.ac.uk/pdbsum/1oco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oco ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COX1_BOVIN COX1_BOVIN] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
== 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/oc/1oco_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=1oco ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme.


==About this Structure==
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.,Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, Inoue N, Yao M, Fei MJ, Libeu CP, Mizushima T, Yamaguchi H, Tomizaki T, Tsukihara T Science. 1998 Jun 12;280(5370):1723-9. PMID:9624044<ref>PMID:9624044</ref>
1OCO is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with CU, MG, NA, ZN, HEA and CMO as [[http://en.wikipedia.org/wiki/ligands ligands]]. The following pages contain interesting information on the relation of 1OCO with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb5_1.html Cytochrome c Oxidase]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OCO OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase., Yoshikawa S, Shinzawa-Itoh K, Nakashima R, Yaono R, Yamashita E, Inoue N, Yao M, Fei MJ, Libeu CP, Mizushima T, Yamaguchi H, Tomizaki T, Tsukihara T, Science. 1998 Jun 12;280(5370):1723-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9624044 9624044]
</div>
<div class="pdbe-citations 1oco" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Cytochrome c]]
[[Category: Cytochrome c]]
[[Category: Cytochrome c Oxidase]]
[[Category: Cytochrome c Oxidase]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Tsukihara, T.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Yao, M.]]
[[Category: Tsukihara T]]
[[Category: CMO]]
[[Category: Yao M]]
[[Category: CU]]
[[Category: HEA]]
[[Category: MG]]
[[Category: NA]]
[[Category: ZN]]
[[Category: carbon monoxide-bound]]
[[Category: cytochrome c oxidase]]
[[Category: oxidoreductase (cytochrome(c)-oxygen)]]
 
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