ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Identification of DksA as a novel pro-inflammatory mediator ofVirulence · 2026Article
- Structural and functional insights into Pseudomonas aeruginosa's secretion systems 1-6: regulation, role in microbial keratitis and drug targets.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Review
- Structure classification of the proteins from Salmonella enterica pangenome revealed novel potential pathogenicity islands.Scientific reports · 2024Article
- Structure and Activity of the Type VI Secretion System.Microbiology spectrum · 2019Review
- Article
- Type VI secretion system: secretion by a contractile nanomachine.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- A disordered region in the EvpP protein from the type VI secretion system of Edwardsiella tarda is essential for EvpC binding.PloS one · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type VI secretion system of Pseudomonas aeruginosa has been shown to be responsible for the translocation of bacteriolytic effectors into competing bacteria. A mechanistic understanding of this widely distributed secretion system is developing and structural studies of its components are ongoing. Two representative structures of one highly conserved component, TssJ, from Escherichia coli and Serratia marcescens have been published. Here, the X-ray crystal structure of TssJ1 from P. aeruginosa is presented at 1.4 Å resolution. The overall structure is conserved among the three proteins. This finding suggests that the homologues function in a similar manner and bolsters the understanding of the structure of this family of proteins.
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