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http://purl.uniprot.org/citations/25275011http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25275011http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25275011http://www.w3.org/2000/01/rdf-schema#comment"Nearly 10% of the coding capacity of the Mycobacterium tuberculosis genome is devoted to two highly expanded and enigmatic protein families called PE and PPE, some of which are important virulence/immunogenicity factors and are secreted during infection via a unique alternative secretory system termed "type VII." How PE-PPE proteins function during infection and how they are translocated to the bacterial surface through the five distinct type VII secretion systems [ESAT-6 secretion system (ESX)] of M. tuberculosis is poorly understood. Here, we report the crystal structure of a PE-PPE heterodimer bound to ESX secretion-associated protein G (EspG), which adopts a novel fold. This PE-PPE-EspG complex, along with structures of two additional EspGs, suggests that EspG acts as an adaptor that recognizes specific PE-PPE protein complexes via extensive interactions with PPE domains, and delivers them to ESX machinery for secretion. Surprisingly, secretion of most PE-PPE proteins in M. tuberculosis is likely mediated by EspG from the ESX-5 system, underscoring the importance of ESX-5 in mycobacterial pathogenesis. Moreover, our results indicate that PE-PPE domains function as cis-acting targeting sequences that are read out by EspGs, revealing the molecular specificity for secretion through distinct ESX pathways."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1409345111"xsd:string
http://purl.uniprot.org/citations/25275011http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1409345111"xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/author"Cox J.S."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/author"Cox J.S."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/author"Ekiert D.C."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/author"Ekiert D.C."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/pages"14758-14763"xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/pages"14758-14763"xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/title"Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/title"Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion."xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/volume"111"xsd:string
http://purl.uniprot.org/citations/25275011http://purl.uniprot.org/core/volume"111"xsd:string
http://purl.uniprot.org/citations/25275011http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25275011
http://purl.uniprot.org/citations/25275011http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25275011
http://purl.uniprot.org/citations/25275011http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25275011
http://purl.uniprot.org/citations/25275011http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25275011
http://purl.uniprot.org/uniprot/A0QQ45http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/25275011
http://purl.uniprot.org/uniprot/P9WJC7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/25275011