ArticleActa crystallographica. Section F, Structural biology communications2016
1.65 Å resolution structure of the AraC-family transcriptional activator ToxT from Vibrio cholerae.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Gut microbiota-derived short-chain fatty acids (SCFAs): immunomodulatory effects and therapeutic potential in infections.Clinical microbiology reviews · 2026Review
- A Twist of Fate: The Helix-Turn-Helix Motif inJournal of chemical information and modeling · 2025Article
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- Structural Insights into Regulation of Vibrio Virulence Gene Networks.Advances in experimental medicine and biology · 2023Article
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- Optimised Heterologous Expression and Functional Analysis of theInternational journal of molecular sciences · 2021Article
- Structural basis for virulence regulation inCommunications biology · 2019Article
- Regulatory Hierarchies Controlling Virulence Gene Expression inFrontiers in microbiology · 2018Review
- Functional Mechanism of the Efflux Pumps Transcription Regulators FromFrontiers in molecular biosciences · 2018Review
- The Fatty Acid Regulator FadR Influences the Expression of the Virulence Cascade in the El Tor Biotype of Vibrio cholerae by Modulating the Levels of ToxT via Two Different Mechanisms.Journal of bacteriology · 2017Article
- A new class of inhibitors of the AraC family virulence regulator Vibrio cholerae ToxT.Scientific reports · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
ToxT is an AraC-family transcriptional activator protein that controls the expression of key virulence factors in Vibrio cholerae, the causative agent of cholera. ToxT directly activates the expression of the genes that encode the toxin-coregulated pilus and cholera toxin, and also positively auto-regulates its own expression from the tcp promoter. The crystal structure of ToxT has previously been solved at 1.9 Å resolution (PDB entry 3gbg). In this study, a crystal structure of ToxT at 1.65 Å resolution with a similar overall structure to the previously determined structure is reported. However, there are distinct differences between the two structures, particularly in the region that extends from Asp101 to Glu110. This region, which can influence ToxT activity but was disordered in the previous structure, can be traced entirely in the current structure.
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