ArticleProceedings of the National Academy of Sciences of the United States of America2005
Predicted hexameric structure of the Agrobacterium VirB4 C terminus suggests VirB4 acts as a docking site during type IV secretion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 57 citations in OpenAlex.
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- Membrane association and polar localization of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Type IV Coupling Proteins as Potential Targets to Control the Dissemination of Antibiotic Resistance.Frontiers in molecular biosciences · 2020Review
- From conjugation to T4S systems in Gram-negative bacteria: a mechanistic biology perspective.EMBO reports · 2019Review
- The Mosaic Type IV Secretion Systems.EcoSal Plus · 2016Review
- Article
- The hexameric structure of a conjugative VirB4 protein ATPase provides new insights for a functional and phylogenetic relationship with DNA translocases.The Journal of biological chemistry · 2012Article
- Enterococcus faecalis PrgJ, a VirB4-like ATPase, mediates pCF10 conjugative transfer through substrate binding.Journal of bacteriology · 2012Article
- Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Mobile genetic elements in the genus Bacteroides, and their mechanism(s) of dissemination.Mobile genetic elements · 2011Article
- Autoinhibitory regulation of TrwK, an essential VirB4 ATPase in type IV secretion systems.The Journal of biological chemistry · 2011Article
- GI-type T4SS-mediated horizontal transfer of the 89K pathogenicity island in epidemic Streptococcus suis serotype 2.Molecular microbiology · 2011Article
- Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system.BMC structural biology · 2011Article
- Evidence for VirB4-mediated dislocation of membrane-integrated VirB2 pilin during biogenesis of the Agrobacterium VirB/VirD4 type IV secretion system.Journal of bacteriology · 2010Article
- Biochemical dissection of the ATPase TraB, the VirB4 homologue of the Escherichia coli pKM101 conjugation machinery.Journal of bacteriology · 2010Article
- Biological diversity of prokaryotic type IV secretion systems.Microbiology and molecular biology reviews : MMBR · 2009Review
- The putative coupling protein TcpA interacts with other pCW3-encoded proteins to form an essential part of the conjugation complex.Journal of bacteriology · 2009Article
- Article
- ATPase activity and oligomeric state of TrwK, the VirB4 homologue of the plasmid R388 type IV secretion system.Journal of bacteriology · 2008Article
- Interaction of Bacteroides fragilis pLV22a relaxase and transfer DNA with Escherichia coli RP4-TraG coupling protein.Molecular microbiology · 2007Article
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5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Agrobacterium T-DNA transporter belongs to a growing class of evolutionarily conserved transporters, called type IV secretion systems (T4SSs). VirB4, 789 aa, is the largest T4SS component, providing a rich source of possible structural domains. Here, we use a variety of bioinformatics methods to predict that the C-terminal domain of VirB4 (including the Walker A and B nucleotide-binding motifs) is related by divergent evolution to the cytoplasmic domain of TrwB, the coupling protein required for conjugative transfer of plasmid R388 from Escherichia coli. This prediction is supported by detailed sequence and structure analyses showing conservation of functionally and structurally important residues between VirB4 and TrwB. The availability of a solved crystal structure for TrwB enables the construction of a comparative model for VirB4 and the prediction that, like TrwB, VirB4 forms a hexamer. These results lead to a model in which VirB4 acts as a docking site at the entrance of the T4SS channel and acts in concert with VirD4 and VirB11 to transport substrates (T-strand linked to VirD2 or proteins such as VirE2, VirE3, or VirF) through the T4SS.
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