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http://purl.uniprot.org/citations/32783951http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32783951http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32783951http://www.w3.org/2000/01/rdf-schema#comment"The 26S proteasome is specialized for regulated protein degradation and formed by a dynamic regulatory particle (RP) that caps a hollow cylindrical core particle (CP) where substrates are proteolyzed. Its diverse substrates unify as proteasome targets by ubiquitination. We used cryogenic electron microscopy (cryo-EM) to study how human 26S proteasome interacts with M1-linked hexaubiquitin (M1-Ub6) unanchored to a substrate and E3 ubiquitin ligase E6AP/UBE3A. Proteasome structures are available with model substrates extending through the RP ATPase ring and substrate-conjugated K63-linked ubiquitin chains present at inhibited deubiquitinating enzyme hRpn11 and the nearby ATPase hRpt4/hRpt5 coiled coil. In this study, we find M1-Ub6 at the hRpn11 site despite the absence of conjugated substrate, indicating that ubiquitin binding at this location does not require substrate interaction with the RP. Moreover, unanchored M1-Ub6 binds to this hRpn11 site of the proteasome with the CP gating residues in both the closed and opened conformational states."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2020.07.011"xsd:string
http://purl.uniprot.org/citations/32783951http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2020.07.011"xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Huang R.K."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Huang R.K."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Zhang P."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Zhang P."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Shi D."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Shi D."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Williams D."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Williams D."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Walters K.J."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Walters K.J."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Fox T."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Fox T."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"de Val N."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"de Val N."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Dorris Z."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Dorris Z."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Khant H."xsd:string
http://purl.uniprot.org/citations/32783951http://purl.uniprot.org/core/author"Khant H."xsd:string