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http://purl.uniprot.org/citations/27562955http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27562955http://www.w3.org/2000/01/rdf-schema#comment"The activated spliceosome (Bact) is in a catalytically inactive state and is remodeled into a catalytically active machine by the RNA helicase Prp2, but the mechanism is unclear. Here, we describe a 3D electron cryomicroscopy structure of the Saccharomyces cerevisiae Bact complex at 5.8-angstrom resolution. Our model reveals that in Bact, the catalytic U2/U6 RNA-Prp8 ribonucleoprotein core is already established, and the 5' splice site (ss) is oriented for step 1 catalysis but occluded by protein. The first-step nucleophile-the branchsite adenosine-is sequestered within the Hsh155 HEAT domain and is held 50 angstroms away from the 5'ss. Our structure suggests that Prp2 adenosine triphosphatase-mediated remodeling leads to conformational changes in Hsh155's HEAT domain that liberate the first-step reactants for catalysis."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.org/dc/terms/identifier"doi:10.1126/science.aag1906"xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Stark H."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Kumar V."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Fabrizio P."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Kastner B."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Luhrmann R."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Chari A."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Lee C.T."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Pena V."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Dybkov O."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Hartmuth K."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/author"Rauhut R."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/pages"1399-1405"xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/title"Molecular architecture of the Saccharomyces cerevisiae activated spliceosome."xsd:string
http://purl.uniprot.org/citations/27562955http://purl.uniprot.org/core/volume"353"xsd:string
http://purl.uniprot.org/citations/27562955http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27562955
http://purl.uniprot.org/citations/27562955http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27562955
http://purl.uniprot.org/uniprot/#_P0C074-mappedCitation-27562955http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27562955
http://purl.uniprot.org/uniprot/#_Q07930-mappedCitation-27562955http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27562955
http://purl.uniprot.org/uniprot/#_P20095-mappedCitation-27562955http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27562955