5z62

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'''Unreleased structure'''
 
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The entry 5z62 is ON HOLD
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==Structure of human cytochrome c oxidase==
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<SX load='5z62' size='340' side='right' viewer='molstar' caption='[[5z62]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5z62]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z62 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#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=CDL:CARDIOLIPIN'>CDL</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=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=5z62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z62 OCA], [https://pdbe.org/5z62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z62 RCSB], [https://www.ebi.ac.uk/pdbsum/5z62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z62 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/COX1_HUMAN COX1_HUMAN] Mitochondrial non-syndromic sensorineural deafness with susceptibility to aminoglycoside exposure;Mitochondrial non-syndromic sensorineural deafness;Genetic recurrent myoglobinuria;Isolated cytochrome C oxidase deficiency;Leber hereditary optic neuropathy;MELAS. The disease is caused by mutations affecting the gene represented in this entry. MT-CO1 may play a role in the pathogenesis of acquired idiopathic sideroblastic anemia, a disease characterized by inadequate formation of heme and excessive accumulation of iron in mitochondria. Mitochondrial iron overload may be attributable to mutations of mitochondrial DNA because these can cause respiratory chain dysfunction, thereby impairing reduction of ferric iron to ferrous iron. The reduced form of iron is essential to the last step of mitochondrial heme biosynthesis.<ref>PMID:9389715</ref> <ref>PMID:9851701</ref> The disease is caused by mutations affecting the gene represented in this entry. The gene represented in this entry may be involved in disease pathogenesis. The disease is caused by mutations affecting the gene represented in this entry. The gene represented in this entry may be involved in disease pathogenesis.
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== Function ==
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[https://www.uniprot.org/uniprot/COX1_HUMAN COX1_HUMAN] 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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Respiration is one of the most basic features of living organisms, and the electron transport chain complexes are probably the most complicated protein system in mitochondria. Complex-IV is the terminal enzyme of the electron transport chain, existing either as randomly scattered complexes or as a component of supercomplexes. NDUFA4 was previously assumed as a subunit of complex-I, but recent biochemical data suggested it may be a subunit of complex-IV. However, no structural evidence supporting this notion was available till now. Here we obtained the 3.3 A resolution structure of complex-IV derived from the human supercomplex I1III2IV1 and assigned the NDUFA4 subunit into complex-IV. Intriguingly, NDUFA4 lies exactly at the dimeric interface observed in previously reported crystal structures of complex-IV homodimer which would preclude complex-IV dimerization. Combining previous structural and biochemical data shown by us and other groups, we propose that the intact complex-IV is a monomer containing 14 subunits.
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Authors: Gu, J., Zong, S., Wu, M., Yang, M.
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Structure of the intact 14-subunit human cytochrome c oxidase.,Zong S, Wu M, Gu J, Liu T, Guo R, Yang M Cell Res. 2018 Oct;28(10):1026-1034. doi: 10.1038/s41422-018-0071-1. Epub 2018, Jul 20. PMID:30030519<ref>PMID:30030519</ref>
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Description: Structure of human cytochrome c oxidase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Yang, M]]
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<div class="pdbe-citations 5z62" style="background-color:#fffaf0;"></div>
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[[Category: Wu, M]]
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[[Category: Zong, S]]
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==See Also==
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[[Category: Gu, J]]
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*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Gu J]]
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[[Category: Wu M]]
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[[Category: Yang M]]
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[[Category: Zong S]]

Current revision

Structure of human cytochrome c oxidase

5z62, resolution 3.60Å

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OCA

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