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8h8s
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Bovine Heart Cytochrome c Oxidase in the Calcium-bound Fully Reduced State== | |
| + | <StructureSection load='8h8s' size='340' side='right'caption='[[8h8s]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8h8s]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H8S FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEK:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL+(5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE'>PEK</scene>, <scene name='pdbligand=PGV:(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+(11E)-OCTADEC-11-ENOATE'>PGV</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=8h8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h8s OCA], [https://pdbe.org/8h8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h8s RCSB], [https://www.ebi.ac.uk/pdbsum/8h8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h8s 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of bovine cytochrome c oxidase (CcO) shows a sodium ion (Na(+)) bound to the surface of subunit I. Changes in the absorption spectrum of heme a caused by calcium ions (Ca(2+)) are detected as small red shifts, and inhibition of enzymatic activity under low turnover conditions is observed by addition of Ca(2+) in a competitive manner with Na(+). In this study, we determined the crystal structure of Ca(2+)-bound bovine CcO in the oxidized and reduced states at 1.7 A resolution. Although Ca(2+) and Na(+) bound to the same site of oxidized and reduced CcO, they led to different coordination geometries. Replacement of Na(+) with Ca(2+) caused a small structural change in the loop segments near the heme a propionate and formyl groups, resulting in spectral changes in heme a. Redox-coupled structural changes observed in the Ca(2+)-bound form were the same as those previously observed in the Na(+)-bound form, suggesting that binding of Ca(2+) does not severely affect enzymatic function, which depends on these structural changes. The relation between the Ca(2+) binding and the inhibitory effect during slow turnover, as well as the possible role of bound Ca(2+) are discussed. | ||
| - | + | Calcium-bound structure of bovine cytochrome c oxidase.,Muramoto K, Shinzawa-Itoh K Biochim Biophys Acta Bioenerg. 2023 Jan 25;1864(2):148956. doi: , 10.1016/j.bbabio.2023.148956. PMID:36708913<ref>PMID:36708913</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8h8s" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Muramoto K]] | ||
| + | [[Category: Shinzawa-Itoh K]] | ||
Revision as of 06:49, 8 February 2023
Bovine Heart Cytochrome c Oxidase in the Calcium-bound Fully Reduced State
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