Results

RDF/XMLNTriplesTurtleShow queryShare ▶
SubjectPredicateObject
http://purl.uniprot.org/citations/20090900http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20090900http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20090900http://www.w3.org/2000/01/rdf-schema#comment"

Background

The exosome complex is an essential RNA 3'-end processing and degradation machinery. In archaeal organisms, the exosome consists of a catalytic ring and an RNA-binding ring, both of which were previously reported to assume three-fold symmetry.

Methodology/principal findings

Here we report an asymmetric 2.9 A Sulfolobus solfataricus archaeal exosome structure in which the three-fold symmetry is broken due to combined rigid body and thermal motions mainly within the RNA-binding ring. Since increased conformational flexibility was also observed in the RNA-binding ring of the related bacterial PNPase, we speculate that this may reflect an evolutionarily conserved mechanism to accommodate diverse RNA substrates for degradation.

Conclusion/significance

This study clearly shows the dynamic structures within the RNA-binding domains, which provides additional insights on mechanism of asymmetric RNA binding and processing."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0008739"xsd:string
http://purl.uniprot.org/citations/20090900http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0008739"xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/author"Lu C."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/author"Lu C."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/author"Ding F."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/author"Ding F."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/author"Ke A."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/author"Ke A."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/pages"E8739"xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/pages"E8739"xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/title"Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/title"Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring."xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/20090900http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/20090900http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20090900
http://purl.uniprot.org/citations/20090900http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20090900
http://purl.uniprot.org/citations/20090900http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20090900
http://purl.uniprot.org/citations/20090900http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20090900
▶