ArticleActa crystallographica. Section F, Structural biology communications2025
Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus.
Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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Who cites it
3 citing papers in PubMed.
- Structural basis of substrate recognition and membrane association by the bacterial lysyl-phosphatidylglycerol hydrolase AcvB.Communications biology · 2026Article
- The Ti Plasmid-Encoded VirJ Functions as a Lysyl-Phosphatidylglycerol Hydrolase in Agrobacterium tumefaciens.Molecular microbiology · 2026Article
- Lifestyle-associated variation in type IV secretion systems between phytopathogenic and environmentalMicrobial genomics · 2026Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Virulence protein J (VirJ) is a periplasmic protein encoded by the bacterial pathogen Brucella abortus and is important for its virulence. The VirJ homologue AcvB from Agrobacterium tumefaciens was found to be a lysyl-phosphatidylglycerol hydrolase that contains two domains, D1 and D2. Interestingly, both VirJ and AcvB are associated with the type IV secretion system (T4SS) activity in the respective bacteria. To date, no structural information is available for these proteins, limiting our understanding of their function. Here, we have purified, crystallized and determined the crystal structure of the N-terminal domain 1 of VirJ (VirJ
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