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http://purl.uniprot.org/citations/21700214http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21700214http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21700214http://www.w3.org/2000/01/rdf-schema#comment"Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded linker; (2), the C-terminal domain binds a [2Fe-2S] cluster through a previously unknown cysteine binding motif in Fe/S proteins; (3), Mia40 specifically introduces two disulfide bonds in a twin CX(2)C motif of the C-terminal domain; (4), anamorsin and Mia40 interact through an intermolecular disulfide-bonded intermediate; and (5), anamorsin is imported into mitochondria. Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2011.03.015"xsd:string
http://purl.uniprot.org/citations/21700214http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2011.03.015"xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Bertini I."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Bertini I."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Banci L."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Banci L."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Ciofi-Baffoni S."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Ciofi-Baffoni S."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Winkelmann J."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Winkelmann J."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Chatzi A."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Chatzi A."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Tokatlidis K."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Tokatlidis K."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Boscaro F."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Boscaro F."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Mikolajczyk M."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/author"Mikolajczyk M."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/21700214http://purl.uniprot.org/core/name"Chem. Biol."xsd:string