{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["111(32)"],"submitter":["Kubori T"],"pubmed_abstract":["Bacterial type IV secretion systems are evolutionarily related to conjugation systems and play a pivotal role in infection by delivering numerous virulence factors into host cells. Using transmission electron microscopy, we report the native molecular structure of the core complex of the Dot/Icm type IV secretion system encoded by Legionella pneumophila, an intracellular human pathogen. The biochemically isolated core complex, composed of at least five proteins--DotC, DotD, DotF, DotG, and DotH--has a ring-shaped structure. Intriguingly, morphologically distinct premature complexes are formed in the absence of DotG or DotF. Our data suggest that DotG forms a central channel spanning inner and outer membranes. DotF, a component dispensable for type IV secretion, plays a role in efficient embedment of DotG into the functional core complex. These results highlight a common scheme for the biogenesis of transport machinery."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["11804-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4136560"],"repository":["biostudies-literature"],"pubmed_title":["Native structure of a type IV secretion system core complex essential for Legionella pathogenesis."],"pmcid":["PMC4136560"],"pubmed_authors":["Nagai H","Higaki S","Aizawa S","Bui XT","Koike M","Kubori T"],"additional_accession":[]},"is_claimable":false,"name":"Native structure of a type IV secretion system core complex essential for Legionella pathogenesis.","description":"Bacterial type IV secretion systems are evolutionarily related to conjugation systems and play a pivotal role in infection by delivering numerous virulence factors into host cells. Using transmission electron microscopy, we report the native molecular structure of the core complex of the Dot/Icm type IV secretion system encoded by Legionella pneumophila, an intracellular human pathogen. The biochemically isolated core complex, composed of at least five proteins--DotC, DotD, DotF, DotG, and DotH--has a ring-shaped structure. Intriguingly, morphologically distinct premature complexes are formed in the absence of DotG or DotF. Our data suggest that DotG forms a central channel spanning inner and outer membranes. DotF, a component dispensable for type IV secretion, plays a role in efficient embedment of DotG into the functional core complex. These results highlight a common scheme for the biogenesis of transport machinery.","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Aug","modification":"2025-04-19T11:18:41.323Z","creation":"2019-03-27T01:34:16Z"},"accession":"S-EPMC4136560","cross_references":{"pubmed":["25062693"],"doi":["10.1073/pnas.1404506111"]}}