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6nl3

From Proteopedia

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Current revision

Solution structure of human Coa6

Structural highlights

6nl3 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

COA6_HUMAN Fatal infantile cytochrome C oxidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.

Function

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.^[1] ^[2] ^[3]

Publication Abstract from PubMed

In eukaryotes, cellular respiration is driven by mitochondrial cytochrome c oxidase (CcO), an enzyme complex that requires copper cofactors for its catalytic activity. Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6, a recently discovered protein whose molecular function is unknown. To uncover the molecular mechanism by which COA6 and SCO proteins mediate copper delivery to COX2, we have solved the solution structure of COA6, which reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Finally, our determination of the interaction surfaces and reduction potentials of COA6 and its client proteins provides a mechanism of how metallochaperone and disulfide reductase activities are coordinated to deliver copper to CcO.

COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase.,Soma S, Morgada MN, Naik MT, Boulet A, Roesler AA, Dziuba N, Ghosh A, Yu Q, Lindahl PA, Ames JB, Leary SC, Vila AJ, Gohil VM Cell Rep. 2019 Dec 17;29(12):4114-4126.e5. doi: 10.1016/j.celrep.2019.11.054. PMID:31851937^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ghosh A, Trivedi PP, Timbalia SA, Griffin AT, Rahn JJ, Chan SS, Gohil VM. Copper supplementation restores cytochrome c oxidase assembly defect in a mitochondrial disease model of COA6 deficiency. Hum Mol Genet. 2014 Jul 1;23(13):3596-606. doi: 10.1093/hmg/ddu069. Epub 2014 Feb, 18. PMID:24549041 doi:http://dx.doi.org/10.1093/hmg/ddu069
↑ Pacheu-Grau D, Bareth B, Dudek J, Juris L, Vogtle FN, Wissel M, Leary SC, Dennerlein S, Rehling P, Deckers M. Cooperation between COA6 and SCO2 in COX2 maturation during cytochrome c oxidase assembly links two mitochondrial cardiomyopathies. Cell Metab. 2015 Jun 2;21(6):823-33. doi: 10.1016/j.cmet.2015.04.012. Epub 2015, May 7. PMID:25959673 doi:http://dx.doi.org/10.1016/j.cmet.2015.04.012
↑ Stroud DA, Maher MJ, Lindau C, Vogtle FN, Frazier AE, Surgenor E, Mountford H, Singh AP, Bonas M, Oeljeklaus S, Warscheid B, Meisinger C, Thorburn DR, Ryan MT. COA6 is a mitochondrial complex IV assembly factor critical for biogenesis of mtDNA-encoded COX2. Hum Mol Genet. 2015 Oct 1;24(19):5404-15. doi: 10.1093/hmg/ddv265. Epub 2015 Jul , 9. PMID:26160915 doi:http://dx.doi.org/10.1093/hmg/ddv265
↑ Soma S, Morgada MN, Naik MT, Boulet A, Roesler AA, Dziuba N, Ghosh A, Yu Q, Lindahl PA, Ames JB, Leary SC, Vila AJ, Gohil VM. COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase. Cell Rep. 2019 Dec 17;29(12):4114-4126.e5. doi: 10.1016/j.celrep.2019.11.054. PMID:31851937 doi:http://dx.doi.org/10.1016/j.celrep.2019.11.054

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6nl3"

Categories: Homo sapiens | Large Structures | Gohil V | Naik MT | Soma S

@@ Line 1: / Line 1: @@
 ==Solution structure of human Coa6==
-<StructureSection load='6nl3' size='340' side='right'caption='[[6nl3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6nl3' size='340' side='right'caption='[[6nl3]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6nl3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NL3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6nl3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NL3 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COA6, C1orf31 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=6nl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nl3 OCA], [https://pdbe.org/6nl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nl3 RCSB], [https://www.ebi.ac.uk/pdbsum/6nl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nl3 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nl3 OCA], [http://pdbe.org/6nl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nl3 RCSB], [http://www.ebi.ac.uk/pdbsum/6nl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nl3 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://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.
+[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 ==
-[[http://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>
+[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 ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Gohil, V]]
+[[Category: Gohil V]]
-[[Category: Naik, M T]]
+[[Category: Naik MT]]
-[[Category: Soma, S]]
+[[Category: Soma S]]
-[[Category: Mitochondrial protein]]
-[[Category: Oxidoreductase]]

6nl3

From Proteopedia

Current revision

Solution structure of human Coa6

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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