ArticleJournal of bacteriology2015
Structural Features Reminiscent of ATP-Driven Protein Translocases Are Essential for the Function of a Type III Secretion-Associated ATPase.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Structure classification of the proteins from Salmonella enterica pangenome revealed novel potential pathogenicity islands.Scientific reports · 2024Article
- Delineating specific regions of N- terminal domain of T3SS ATPase YsaN ofFrontiers in molecular biosciences · 2022Article
- Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.Protein science : a publication of the Protein Society · 2019Article
- Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase FromFrontiers in microbiology · 2018Article
- Visualization and characterization of individual type III protein secretion machines in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural and Biochemical Characterization of Spa47 Provides Mechanistic Insight into Type III Secretion System ATPase Activation and Shigella Virulence Regulation.The Journal of biological chemistry · 2016Article
- Antibacterial Flavonoids from Medicinal Plants Covalently Inactivate Type III Protein Secretion Substrates.Journal of the American Chemical Society · 2016Article
- The Agrobacterium VirB/VirD4 T4SS: Mechanism and Architecture Defined Through In Vivo Mutagenesis and Chimeric Systems.Current topics in microbiology and immunologyReview
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
unlabelledMany bacterial pathogens and symbionts utilize type III secretion systems to interact with their hosts. These machines have evolved to deliver bacterial effector proteins into eukaryotic target cells to modulate a variety of cellular functions. One of the most conserved components of these systems is an ATPase, which plays an essential role in the recognition and unfolding of proteins destined for secretion by the type III pathway. Here we show that structural features reminiscent of other ATP-driven protein translocases are essential for the function of InvC, the ATPase associated with a Salmonella enterica serovar Typhimurium type III secretion system. Mutational and functional analyses showed that a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase are essential for InvC function. These findings provide mechanistic insight into the function of this highly conserved component of type III secretion machines. IMPORTANCE: Type III secretion machines are essential for the virulence or symbiotic relationships of many bacteria. These machines have evolved to deliver bacterial effector proteins into host cells to modulate cellular functions, thus facilitating bacterial colonization and replication. An essential component of these machines is a highly conserved ATPase, which is necessary for the recognition and secretion of proteins destined to be delivered by the type III secretion pathway. Using modeling and structure and function analyses, we have identified structural features of one of these ATPases from Salmonella enterica serovar Typhimurium that help to explain important aspects of its function.
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