9i7u: Difference between revisions

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New page: '''Unreleased structure''' The entry 9i7u is ON HOLD until sometime in the future Authors: Nguyen, M.D., Singh, V., Rorbach, J. Description: Cryo-EM structure of NDUFA4 bound complex I...
 
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'''Unreleased structure'''


The entry 9i7u is ON HOLD  until sometime in the future
==Cryo-EM structure of NDUFA4 bound complex IV within the respirasome complex==
 
<StructureSection load='9i7u' size='340' side='right'caption='[[9i7u]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
Authors: Nguyen, M.D., Singh, V., Rorbach, J.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9i7u]] 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=9I7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9I7U FirstGlance]. <br>
Description: Cryo-EM structure of NDUFA4 bound complex IV within the respirasome complex
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.15&#8491;</td></tr>
[[Category: Unreleased Structures]]
<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=FME:N-FORMYLMETHIONINE'>FME</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=PGV:(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+(11E)-OCTADEC-11-ENOATE'>PGV</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Nguyen, M.D]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9i7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9i7u OCA], [https://pdbe.org/9i7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9i7u RCSB], [https://www.ebi.ac.uk/pdbsum/9i7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9i7u ProSAT]</span></td></tr>
[[Category: Rorbach, J]]
</table>
[[Category: Singh, V]]
== Disease ==
[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.
== Function ==
[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.
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Nguyen MD]]
[[Category: Rorbach J]]
[[Category: Singh V]]
Retrieved from "https://proteopedia.org/9i7u"