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http://purl.uniprot.org/citations/25703377http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25703377http://www.w3.org/2000/01/rdf-schema#comment"Ddi1 belongs to a family of shuttle proteins targeting polyubiquitinated substrates for proteasomal degradation. Unlike the other proteasomal shuttles, Rad23 and Dsk2, Ddi1 remains an enigma: its function is not fully understood and structural properties are poorly characterized. We determined the structure and binding properties of the ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains of Ddi1 from Saccharomyces cerevisiae. We found that while Ddi1UBA forms a characteristic UBA:ubiquitin complex, Ddi1UBL has entirely uncharacteristic binding preferences. Despite having a ubiquitin-like fold, Ddi1UBL does not interact with typical UBL receptors but unexpectedly binds ubiquitin, forming a unique interface mediated by hydrophobic contacts and by salt bridges between oppositely charged residues of Ddi1UBL and ubiquitin. In stark contrast to ubiquitin and other UBLs, the β-sheet surface of Ddi1UBL is negatively charged and therefore is recognized in a completely different way. The dual functionality of Ddi1UBL, capable of binding both ubiquitin and proteasome, suggests an intriguing mechanism for Ddi1 as a proteasomal shuttle."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2015.01.010"xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Zhang D."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Chen T.Y."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Fushman D."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Glickman M.H."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Reis N."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Krutauz D."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Walker O."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Nowicka U."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Chaturvedi A."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/author"Castaneda C.A."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/pages"542-557"xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/title"DNA-damage-inducible 1 protein (Ddi1) contains an uncharacteristic ubiquitin-like domain that binds ubiquitin."xsd:string
http://purl.uniprot.org/citations/25703377http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/25703377http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25703377
http://purl.uniprot.org/citations/25703377http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25703377
http://purl.uniprot.org/uniprot/#_A0A6A5Q0F6-mappedCitation-25703377http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25703377
http://purl.uniprot.org/uniprot/#_P40087-mappedCitation-25703377http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25703377
http://purl.uniprot.org/uniprot/#_P0CG47-mappedCitation-25703377http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25703377
http://purl.uniprot.org/uniprot/#_P0CG48-mappedCitation-25703377http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25703377
http://purl.uniprot.org/uniprot/P0CG47http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25703377