View source for 6pcf


==Human Coa6: W59C mutant protein==
<StructureSection load='6pcf' size='340' side='right'caption='[[6pcf]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pcf]] is a 4 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=6PCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PCF 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]] 2.2&#8491;</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=6pcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pcf OCA], [https://pdbe.org/6pcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pcf RCSB], [https://www.ebi.ac.uk/pdbsum/6pcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pcf ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/COA6_HUMAN COA6_HUMAN] Fatal infantile cytochrome C oxidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/COA6_HUMAN COA6_HUMAN] Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV.<ref>PMID:24549041</ref> <ref>PMID:25959673</ref> <ref>PMID:26160915</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Assembly factors play key roles in the biogenesis of many multi-subunit protein complexes regulating their stability, activity, and the incorporation of essential cofactors. The human assembly factor Coa6 participates in the biogenesis of the CuA site in complex IV (cytochrome c oxidase, COX). Patients with mutations in Coa6 suffer from mitochondrial disease due to complex IV deficiency. Here, we present the crystal structures of human Coa6 and the pathogenic (W59C)Coa6-mutant protein. These structures show that Coa6 has a 3-helical bundle structure, with the first 2 helices tethered by disulfide bonds, one of which likely provides the copper-binding site. Disulfide-mediated oligomerization of the (W59C)Coa6 protein provides a structural explanation for the loss-of-function mutation.

Structural and functional characterization of the mitochondrial complex IV assembly factor Coa6.,Maghool S, Cooray NDG, Stroud DA, Aragao D, Ryan MT, Maher MJ Life Sci Alliance. 2019 Sep 12;2(5). pii: 2/5/e201900458. doi:, 10.26508/lsa.201900458. Print 2019 Oct. PMID:31515291<ref>PMID:31515291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pcf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Maghool S]]
[[Category: Maher MJ]]