ArticleBMC structural biology2011
Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system.
Article in BMC structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- Structural Diversity of Native Major Ampullate, Minor Ampullate, Cylindriform, and Flagelliform Silk Proteins in Solution.Biomacromolecules · 2020Article
- A unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel.Nature microbiology · 2018Article
- The Tiam1 guanine nucleotide exchange factor is auto-inhibited by its pleckstrin homology coiled-coil extension domain.The Journal of biological chemistry · 2017Article
- Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.The EMBO journal · 2017Article
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- Structural organisation of the type IV secretion systems.Current opinion in microbiology · 2014Review
- Review
- Surface organelles assembled by secretion systems of Gram-negative bacteria: diversity in structure and function.FEMS microbiology reviews · 2012Review
- 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
- Autoinhibitory regulation of TrwK, an essential VirB4 ATPase in type IV secretion systems.The Journal of biological chemistry · 2011Article
- The expanding bacterial type IV secretion lexicon.Research in microbiologyReview
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3 authors.
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Abstract
backgroundType IV secretion (T4S) systems are involved in secretion of virulence factors such as toxins or transforming molecules, or bacterial conjugation. T4S systems are composed of 12 proteins named VirB1-B11 and VirD4. Among them, three ATPases are involved in the assembly of the T4S system and/or provide energy for substrate transfer, VirB4, VirB11 and VirD4. The X-ray crystal structures of VirB11 and VirD4 have already been solved but VirB4 has proven to be reluctant to any structural investigation so far.
resultsHere, we have used small-angle X-ray scattering to obtain the first structural models for the membrane-extracted, dimeric form of the TraB protein, the VirB4 homolog encoded by the E. coli pKM101 plasmid, and for the monomeric soluble form of the LvhB4 protein, the VirB4 homolog of the T4S system encoded by the Legionella pneumophila lvh operon. We have obtained the low resolution structures of the full-length TraB and of its N- and C-terminal halves. From these SAXS models, we derive the internal organisation of TraB. We also show that the two TraB N- and C-terminal domains are independently involved in the dimerisation of the full-length protein.
conclusionsThese models provide the first structural insights into the architecture of VirB4 proteins. In particular, our results highlight the modular arrangement and functional relevance of the dimeric-membrane-bound form of TraB.
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