RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17766440http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17766440http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17766440http://www.w3.org/2000/01/rdf-schema#comment"Iron-sulfur (Fe-S) proteins are key players in vital processes involving energy homeostasis and metabolism from the simplest to most complex organisms. We report a 1.5 A x-ray crystal structure of the first identified outer mitochondrial membrane Fe-S protein, mitoNEET. Two protomers intertwine to form a unique dimeric structure that constitutes a new fold to not only the approximately 650 reported Fe-S protein structures but also to all known proteins. We name this motif the NEET fold. The protomers form a two-domain structure: a beta-cap domain and a cluster-binding domain that coordinates two acid-labile 2Fe-2S clusters. Binding of pioglitazone, an insulin-sensitizing thiazolidinedione used in the treatment of type 2 diabetes, stabilizes the protein against 2Fe-2S cluster release. The biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe-S cluster transfer."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0707189104"xsd:string
http://purl.uniprot.org/citations/17766440http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0707189104"xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Axelrod H.L."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Axelrod H.L."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Dixon J.E."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Dixon J.E."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Wiley S.E."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Wiley S.E."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Roy M."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Roy M."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Jennings P.A."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Jennings P.A."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Nechushtai R."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Nechushtai R."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Paddock M.L."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Paddock M.L."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Abresch E.C."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Abresch E.C."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Capraro D."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Capraro D."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Cohen A.E."xsd:string
http://purl.uniprot.org/citations/17766440http://purl.uniprot.org/core/author"Cohen A.E."xsd:string