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1.65Å resolution structure of the AraC-family transcriptional activator ToxT from Vibrio cholerae

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-r...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2016-09, Vol.72 (9), p.726
Main Authors: Li, Jiaqin, Wehmeyer, Graham, Lovell, Scott, Battaile, Kevin P, Egan, Susan M
Format: Article
Language:English
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Summary: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 1.9Å resolution (PDB entry 3gbg). In this study, a crystal structure of ToxT at 1.65Å 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.
ISSN:2053-230X
DOI:10.1107/S2053230X1601298X