ArticleJournal of microbiology (Seoul, Korea)2015
Crystal structure of the bacterial type VI secretion system component TssL from Vibrio cholerae.
Article in Journal of microbiology (Seoul, Korea), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed.
- Structure and Function of the Dot/Icm T4SS.bioRxiv : the preprint server for biology · 2023Article
- Structural Characterization of TssL from Acinetobacter baumannii: a Key Component of the Type VI Secretion System.Journal of bacteriology · 2020Article
- 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
- Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type VI secretion system (T6SS), commonly found in gram-negative bacteria, is responsible for exporting effector proteins. The T6SS has been reported to be cytotoxic to host cells. While the components and assembly of the T6SS complex have been largely assessed, structural data on T6SS components from virulent bacteria is remarkably insufficient. Here, we report the crystal structure of Vibrio cholerae TssL (VcTssL), a core component of T6SS. In spite of a relatively low sequence identity, the overall structure of VcTssL is largely similar to those from other bacterial homologs except for several differences found in local structural elements. A unique feature attributed to the C-terminal fragment of VcTssL is a crystallographic artifact. This incidental feature of VcTssL may provide insights into screening of molecular partners for the cytoplasmic domain of TssL. Additionally, our results may help in the design of molecular probes for a detailed understanding of the functional relationship between TssL and other T6SS components.
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