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http://purl.uniprot.org/citations/31264960http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31264960http://www.w3.org/2000/01/rdf-schema#comment"Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule."xsd:string
http://purl.uniprot.org/citations/31264960http://purl.org/dc/terms/identifier"doi:10.7554/elife.47145"xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/author"He S."xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/author"Scheres S.H."xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/author"Carter A.P."xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/author"Lacey S.E."xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/pages"e47145"xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/title"Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule."xsd:string
http://purl.uniprot.org/citations/31264960http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/31264960http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31264960
http://purl.uniprot.org/citations/31264960http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31264960
http://purl.uniprot.org/uniprot/#_P02554-mappedCitation-31264960http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31264960
http://purl.uniprot.org/uniprot/#_Q2XVP4-mappedCitation-31264960http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31264960
http://purl.uniprot.org/uniprot/#_Q9JHU4-mappedCitation-31264960http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31264960
http://purl.uniprot.org/uniprot/#_Q8WXX0-mappedCitation-31264960http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31264960
http://purl.uniprot.org/uniprot/P02554http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31264960
http://purl.uniprot.org/uniprot/Q9JHU4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31264960
http://purl.uniprot.org/uniprot/Q8WXX0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31264960
http://purl.uniprot.org/uniprot/Q2XVP4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31264960