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http://purl.uniprot.org/citations/16291742http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16291742http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16291742http://www.w3.org/2000/01/rdf-schema#comment"SOD1 has to undergo several post-translational modifications before reaching its mature form. The protein requires insertion of zinc and copper atoms, followed by the formation of a conserved S-S bond between Cys-57 and Cys-146 (human numbering), which makes the protein fully active. In this report an NMR structural investigation of the reduced SH-SH form of thermostable E,Zn-as-SOD1 (E is empty; as is C6A, C111S) is reported, characterizing the protein just before the last step leading to the mature form. The structure is compared with that of the oxidized S-S form as well as with that of the yeast SOD1 complexed with its copper chaperone, CCS. Local conformational rearrangements upon disulfide bridge reduction are localized in the region near Cys-57 that is completely exposed to the solvent in the present structure, at variance with the oxidized forms. There is a local disorder around Cys-57 that may serve for protein-protein recognition and may possibly be involved in intermolecular S-S bonds in familial amyotrophic lateral sclerosis-related SOD1 mutants. The structure allows us to further discuss the copper loading mechanism in SOD1."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m506497200"xsd:string
http://purl.uniprot.org/citations/16291742http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m506497200"xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Bertini I."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Bertini I."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Banci L."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Banci L."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Cantini F."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Cantini F."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"D'Amelio N."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"D'Amelio N."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Gaggelli E."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/author"Gaggelli E."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/pages"2333-2337"xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/pages"2333-2337"xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/title"Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/title"Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form."xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/16291742http://purl.uniprot.org/core/volume"281"xsd:string