ArticleThe Journal of biological chemistry2012
The hexameric structure of a conjugative VirB4 protein ATPase provides new insights for a functional and phylogenetic relationship with DNA translocases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 71 citations in OpenAlex.
- Evolutionary and Mobile Genetic Element Analysis of a Multidrug-Resistant ST398-MRSA-Vc Isolate from Ready-to-Eat Pork Products.Antibiotics (Basel, Switzerland) · 2026Article
- Type IV secretion systems: from structures to mechanisms.The EMBO journal · 2025Review
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase ofBiomolecules · 2023Article
- Recent advances in structural studies of the Legionella pneumophila Dot/Icm type IV secretion system.Microbiology and immunology · 2022Review
- Multiple relaxases contribute to the horizontal transfer of the virulence plasmids from the tumorigenic bacteriumFrontiers in microbiology · 2022Article
- Structural analysis of VirD4 a type IV ATPase encoded by transmissible plasmids ofFrontiers in artificial intelligence · 2022Article
- VirB4- and VirD4-Like ATPases, Components of a Putative Type 4C Secretion System in Clostridioides difficile.Journal of bacteriology · 2021Article
- Monitoring Bacterial Conjugation by Optical Microscopy.Frontiers in microbiology · 2021Article
- The TraK accessory factor activates substrate transfer through the pKM101 type IV secretion system independently of its role in relaxosome assembly.Molecular microbiology · 2020Article
- Type IV Coupling Proteins as Potential Targets to Control the Dissemination of Antibiotic Resistance.Frontiers in molecular biosciences · 2020Review
- The FtsK-like motor TraB is a DNA-dependent ATPase that forms higher-order assemblies.The Journal of biological chemistry · 2019Article
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
- From conjugation to T4S systems in Gram-negative bacteria: a mechanistic biology perspective.EMBO reports · 2019Review
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.The EMBO journal · 2017Article
- Substrate translocation involves specific lysine residues of the central channel of the conjugative coupling protein TrwB.Molecular genetics and genomics : MGG · 2017Article
- Analyzing the role of CagV, a VirB8 homolog of the type IV secretion system ofFEBS open bio · 2017Article
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8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VirB4 proteins are ATPases essential for pilus biogenesis and protein transport in type IV secretion systems. These proteins contain a motor domain that shares structural similarities with the motor domains of DNA translocases, such as the VirD4/TrwB conjugative coupling proteins and the chromosome segregation pump FtsK. Here, we report the three-dimensional structure of full-length TrwK, the VirB4 homologue in the conjugative plasmid R388, determined by single-particle electron microscopy. The structure consists of a hexameric double ring with a barrel-shaped structure. The C-terminal half of VirB4 proteins shares a striking structural similarity with the DNA translocase TrwB. Docking the atomic coordinates of the crystal structures of TrwB and FtsK into the EM map revealed a better fit for FtsK. Interestingly, we have found that like TrwB, TrwK is able to bind DNA with a higher affinity for G4 quadruplex structures than for single-stranded DNA. Furthermore, TrwK exerts a dominant negative effect on the ATPase activity of TrwB, which reflects an interaction between the two proteins. Our studies provide new insights into the structure-function relationship and the evolution of these DNA and protein translocases.
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