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http://purl.uniprot.org/citations/20937829http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20937829http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20937829http://www.w3.org/2000/01/rdf-schema#comment"Type III secretion systems (TTSSs) utilized by enteropathogenic bacteria require the presence of small, acidic virulence-associated chaperones for effective host cell infection. We adopted a combination of biochemical and cellular techniques to define the chaperone binding domains (CBDs) in the translocators IpaB and IpaC associated with the chaperone IpgC from Shigella flexneri. We identified a novel CBD in IpaB and furthermore precisely mapped the boundaries of the CBDs in both translocator proteins. In IpaC a single binding domain associates with IpgC. In IpaB, we show that the binding of the newly characterized CBD is essential in maintaining the ternary arrangement of chaperone-translocator complex. This hitherto unknown function is reflected in the co-crystal structure as well, with an IpgC dimer bound to an IpaB fragment comprising both CBDs. Moreover, in the absence of this novel CBD the IpaB/IpgC complex aggregates. This dual-recognition of a domain in the protein by the chaperone in facilitating the correct chaperone-substrate organization describes a new function for the TTSS associated chaperone-substrate complexes."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.135616"xsd:string
http://purl.uniprot.org/citations/20937829http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.135616"xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Kolbe M."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Kolbe M."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Lokareddy R.K."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Lokareddy R.K."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Lunelli M."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Lunelli M."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Eilers B."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Eilers B."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Wolter V."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/author"Wolter V."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/pages"39965-39975"xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/pages"39965-39975"xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/title"Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/title"Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB."xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20937829http://purl.uniprot.org/core/volume"285"xsd:string