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http://purl.uniprot.org/citations/17158460http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17158460http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17158460http://www.w3.org/2000/01/rdf-schema#comment"Folding and assembly of endosialidases, the trimeric tail spike proteins of Escherichia coli K1-specific bacteriophages, crucially depend on their C-terminal domain (CTD). Homologous CTDs were identified in phage proteins belonging to three different protein families: neck appendage proteins of several Bacillus phages, L-shaped tail fibers of coliphage T5, and K5 lyases, the tail spike proteins of phages infecting E. coli K5. By analyzing a representative of each family, we show that in all cases, the CTD is cleaved off after a strictly conserved serine residue and alanine substitution prevented cleavage. Further structural and functional analyses revealed that (i) CTDs are autonomous domains with a high alpha-helical content; (ii) proteolytically released CTDs assemble into hexamers, which are most likely dimers of trimers; (iii) highly conserved amino acids within the CTD are indispensable for CTD-mediated folding and complex formation; (iv) CTDs can be exchanged between proteins of different families; and (v) proteolytic cleavage is essential to stabilize the native protein complex. Data obtained for full-length and proteolytically processed endosialidase variants suggest that release of the CTD increases the unfolding barrier, trapping the mature trimer in a kinetically stable conformation. In summary, we characterize the CTD as a novel C-terminal chaperone domain, which assists folding and assembly of unrelated phage proteins."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609543200"xsd:string
http://purl.uniprot.org/citations/17158460http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609543200"xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Gerardy-Schahn R."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Gerardy-Schahn R."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Muehlenhoff M."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Muehlenhoff M."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Schwarzer D."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Schwarzer D."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Stummeyer K."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/author"Stummeyer K."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/pages"2821-2831"xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/pages"2821-2831"xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/title"Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/title"Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins."xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17158460http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17158460http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17158460
http://purl.uniprot.org/citations/17158460http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17158460