ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Metabolic Potential of Candidatus Saccharimonadia Including Rare Lineages in Activated Sludge.Environmental microbiology reports · 2025Article
- The assembly of a hybrid type IV secretion system by a Crohn's disease-associated Escherichia coli strain.Nature communications · 2025Article
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- Expanded geographic distribution for twomSphere · 2024Article
- Membrane association and polar localization of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- 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
- Metabolic versatility ofFrontiers in microbiology · 2023Article
- Cryo-EM structure of a type IV secretion system.Nature · 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
- Secretion of Pertussis Toxin fromToxins · 2021Review
- Incompatibility Group I1 (IncI1) Plasmids: Their Genetics, Biology, and Public Health Relevance.Microbiology and molecular biology reviews : MMBR · 2021Review
- Protein Dynamics in F-like Bacterial Conjugation.Biomedicines · 2020Review
- Unravelling the effects of tropical land use conversion on the soil microbiome.Environmental microbiome · 2020Article
- Structural insights into substrate recognition by the type VII secretion system.Protein & cell · 2020Article
- Type IV Coupling Proteins as Potential Targets to Control the Dissemination of Antibiotic Resistance.Frontiers in molecular biosciences · 2020Review
- 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
- Functional and evolutionary analysis of viral proteins containing a Rossmann-like fold.Protein science : a publication of the Protein Society · 2018Article
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8 authors.
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Abstract
Type IV secretion (T4S) systems mediate the transfer of proteins and DNA across the cell envelope of bacteria. These systems play important roles in bacterial pathogenesis and in horizontal transfer of antibiotic resistance. The VirB4 ATPase of the T4S system is essential for both the assembly of the system and substrate transfer. In this article, we present the crystal structure of the C-terminal domain of Thermoanaerobacter pseudethanolicus VirB4. This structure is strikingly similar to that of another T4S ATPase, VirD4, a protein that shares only 12% sequence identity with VirB4. The VirB4 domain purifies as a monomer, but the full-length protein is observed in a monomer-dimer equilibrium, even in the presence of nucleotides and DNAs. We also report the negative stain electron microscopy structure of the core complex of the T4S system of the Escherichia coli pKM101 plasmid, with VirB4 bound. In this structure, VirB4 is also monomeric and bound through its N-terminal domain to the core's VirB9 protein. Remarkably, VirB4 is observed bound to the side of the complex where it is ideally placed to play its known regulatory role in substrate transfer.
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