<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>111(32)</volume><submitter>Kubori T</submitter><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.</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pagination>11804-9</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4136560</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Native structure of a type IV secretion system core complex essential for Legionella pathogenesis.</pubmed_title><pmcid>PMC4136560</pmcid><pubmed_authors>Nagai H</pubmed_authors><pubmed_authors>Higaki S</pubmed_authors><pubmed_authors>Aizawa S</pubmed_authors><pubmed_authors>Bui XT</pubmed_authors><pubmed_authors>Koike M</pubmed_authors><pubmed_authors>Kubori T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Native structure of a type IV secretion system core complex essential for Legionella pathogenesis.</name><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.</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Aug</publication><modification>2025-04-19T11:18:41.323Z</modification><creation>2019-03-27T01:34:16Z</creation></dates><accession>S-EPMC4136560</accession><cross_references><pubmed>25062693</pubmed><doi>10.1073/pnas.1404506111</doi></cross_references></HashMap>