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http://purl.uniprot.org/citations/31974312http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31974312http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31974312http://www.w3.org/2000/01/rdf-schema#comment"The spliceosome consists of five small RNAs and more than 100 proteins. Almost 50% of the human spliceosomal proteins were predicted to be intrinsically disordered or to contain disordered regions, among them the G-patch protein Spp2. The G-patch region of Spp2 binds to the DEAH-box ATPase Prp2, and both proteins together are essential for promoting the transition from the Bact to the catalytically active B* spliceosome. Here we show by circular dichroism and nuclear magnetic resonance (NMR) spectroscopy that Spp2 is intrinsically disordered in solution. Crystal structures of a complex consisting of Prp2-ADP and the G-patch domain of Spp2 demonstrate that the G-patch gains a defined fold when bound to Prp2. While the N-terminal region of the G-patch always folds into an α-helix in five different crystal structures, the C-terminal part is able to adopt two alternative conformations. NMR studies further revealed that the N-terminal part of the Spp2 G-patch, which is the most conserved region in different G-patch proteins, transiently samples helical conformations, possibly facilitating a conformational selection binding mechanism. The structural analysis unveils the role of conserved residues of the G-patch in the dynamic interaction mode of Spp2 with Prp2, which is vital to maintain the binding during the Prp2 domain movements needed for RNA translocation."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1907960117"xsd:string
http://purl.uniprot.org/citations/31974312http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1907960117"xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Ficner R."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Ficner R."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Schmitt A."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Schmitt A."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Favretto F."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Favretto F."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Neumann P."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Neumann P."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Zweckstetter M."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Zweckstetter M."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Xiang S."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Xiang S."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Hofele R."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Hofele R."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Hamann F."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/author"Hamann F."xsd:string
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/31974312http://purl.uniprot.org/core/date"2020"xsd:gYear