Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein
Human SCO1 and SCO2 are copper-binding proteins involved in the assembly of mitochondrial cytochrome c oxidase (COX). We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 A. It is similar to redox active proteins, including thioredoxins (Trx...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-04, Vol.280 (15), p.15202 |
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| creator | Williams, John C Sue, Carolyn Banting, Graham S Yang, Hua Glerum, D Moira Hendrickson, Wayne A Schon, Eric A |
| description | Human SCO1 and SCO2 are copper-binding proteins involved in the assembly of mitochondrial cytochrome c oxidase (COX). We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 A. It is similar to redox active proteins, including thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding ligands located at the same positions as the conserved catalytic residues in Trx and Prx. SCO1 does not have disulfide isomerization or peroxidase activity, but both hSCO1 and a sco1 null in yeast show extreme sensitivity to hydrogen peroxide. Of the six missense mutations in SCO1 and SCO2 associated with fatal mitochondrial disorders, one lies in a highly conserved exposed surface away from the copper-binding region, suggesting that this region is involved in protein-protein interactions. These data suggests that SCO functions not as a COX copper chaperone, but rather as a mitochondrial redox signaling molecule. |
| doi_str_mv | 10.1074/jbc.M410705200 |
| format | Article |
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We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 A. It is similar to redox active proteins, including thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding ligands located at the same positions as the conserved catalytic residues in Trx and Prx. SCO1 does not have disulfide isomerization or peroxidase activity, but both hSCO1 and a sco1 null in yeast show extreme sensitivity to hydrogen peroxide. Of the six missense mutations in SCO1 and SCO2 associated with fatal mitochondrial disorders, one lies in a highly conserved exposed surface away from the copper-binding region, suggesting that this region is involved in protein-protein interactions. 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We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 A. It is similar to redox active proteins, including thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding ligands located at the same positions as the conserved catalytic residues in Trx and Prx. SCO1 does not have disulfide isomerization or peroxidase activity, but both hSCO1 and a sco1 null in yeast show extreme sensitivity to hydrogen peroxide. Of the six missense mutations in SCO1 and SCO2 associated with fatal mitochondrial disorders, one lies in a highly conserved exposed surface away from the copper-binding region, suggesting that this region is involved in protein-protein interactions. These data suggests that SCO functions not as a COX copper chaperone, but rather as a mitochondrial redox signaling molecule.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Cattle</subject><subject>Chromatography</subject><subject>Copper - chemistry</subject><subject>Crystallography, X-Ray</subject><subject>Cysteine - chemistry</subject><subject>Disulfides - chemistry</subject><subject>Electron Transport Complex IV - chemistry</subject><subject>Genotype</subject><subject>Humans</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Ligands</subject><subject>Membrane Proteins - chemistry</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial Proteins - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Chaperones - chemistry</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Mutation, Missense</subject><subject>Oxidation-Reduction</subject><subject>Peroxidases - chemistry</subject><subject>Peroxides - chemistry</subject><subject>Point Mutation</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Homology, Amino Acid</subject><subject>Thioredoxins - chemistry</subject><subject>Time Factors</subject><issn>0021-9258</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kDtPwzAUhT2AaCmsjOiqe4ofcYLZUMRLKuoAzNW147SukjiyHYlI_HiKgLOc8y3fcAi5YnTFaJnfHLRZvebHSSWn9ITMKeUsU1zezsh5jAd6TK7YGZkxWUglVDEnX1WYYsIWYgqjSWOw4BvYjx328FZt2B24bmidweR8H6HxAYKt_SdEt-uxdf0O9AQInUve7H1fB3eUmemHgu8sGPCfrsZoYYkx2k630xKG4JN1_QU5bbCN9vKvF-Tj8eG9es7Wm6eX6n6dDZyqlBlFBRWITVMiRVWyQnKjeZljLVmuSiWKUhRCWLRCW2E4l0o2tNBoayNqLRbk-tc7jLqz9XYIrsMwbf9vEN9VEl-7</recordid><startdate>20050415</startdate><enddate>20050415</enddate><creator>Williams, John C</creator><creator>Sue, Carolyn</creator><creator>Banting, Graham S</creator><creator>Yang, Hua</creator><creator>Glerum, D Moira</creator><creator>Hendrickson, Wayne A</creator><creator>Schon, Eric A</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20050415</creationdate><title>Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein</title><author>Williams, John C ; Sue, Carolyn ; Banting, Graham S ; Yang, Hua ; Glerum, D Moira ; Hendrickson, Wayne A ; Schon, Eric A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p209t-c90303aaff7a0a971652cb274ad5149793673633eae3be3c22595f06baedc3db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Cattle</topic><topic>Chromatography</topic><topic>Copper - chemistry</topic><topic>Crystallography, X-Ray</topic><topic>Cysteine - chemistry</topic><topic>Disulfides - chemistry</topic><topic>Electron Transport Complex IV - chemistry</topic><topic>Genotype</topic><topic>Humans</topic><topic>Hydrogen Peroxide - chemistry</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Ligands</topic><topic>Membrane Proteins - chemistry</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial Proteins - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular Chaperones - chemistry</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Mutation, Missense</topic><topic>Oxidation-Reduction</topic><topic>Peroxidases - chemistry</topic><topic>Peroxides - chemistry</topic><topic>Point Mutation</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>Sequence Homology, Amino Acid</topic><topic>Thioredoxins - chemistry</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Williams, John C</creatorcontrib><creatorcontrib>Sue, Carolyn</creatorcontrib><creatorcontrib>Banting, Graham S</creatorcontrib><creatorcontrib>Yang, Hua</creatorcontrib><creatorcontrib>Glerum, D Moira</creatorcontrib><creatorcontrib>Hendrickson, Wayne A</creatorcontrib><creatorcontrib>Schon, Eric A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Williams, John C</au><au>Sue, Carolyn</au><au>Banting, Graham S</au><au>Yang, Hua</au><au>Glerum, D Moira</au><au>Hendrickson, Wayne A</au><au>Schon, Eric A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2005-04-15</date><risdate>2005</risdate><volume>280</volume><issue>15</issue><spage>15202</spage><pages>15202-</pages><issn>0021-9258</issn><abstract>Human SCO1 and SCO2 are copper-binding proteins involved in the assembly of mitochondrial cytochrome c oxidase (COX). We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 A. It is similar to redox active proteins, including thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding ligands located at the same positions as the conserved catalytic residues in Trx and Prx. SCO1 does not have disulfide isomerization or peroxidase activity, but both hSCO1 and a sco1 null in yeast show extreme sensitivity to hydrogen peroxide. Of the six missense mutations in SCO1 and SCO2 associated with fatal mitochondrial disorders, one lies in a highly conserved exposed surface away from the copper-binding region, suggesting that this region is involved in protein-protein interactions. These data suggests that SCO functions not as a COX copper chaperone, but rather as a mitochondrial redox signaling molecule.</abstract><cop>United States</cop><pmid>15659396</pmid><doi>10.1074/jbc.M410705200</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Binding Sites Cattle Chromatography Copper - chemistry Crystallography, X-Ray Cysteine - chemistry Disulfides - chemistry Electron Transport Complex IV - chemistry Genotype Humans Hydrogen Peroxide - chemistry Hydrogen Peroxide - pharmacology Ligands Membrane Proteins - chemistry Mitochondria - metabolism Mitochondrial Proteins - chemistry Models, Molecular Molecular Chaperones - chemistry Molecular Sequence Data Mutation Mutation, Missense Oxidation-Reduction Peroxidases - chemistry Peroxides - chemistry Point Mutation Protein Conformation Protein Structure, Tertiary Sequence Homology, Amino Acid Thioredoxins - chemistry Time Factors |
| title | Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein |
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