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

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• 作者：Jiaqin Li ; Graham Wehmeyer ; Scott Lovell ; Kevin P. Battaile and Susan M. Egan
• 关键词：AraC ; ToxT ; Vibrio cholerae ; crystal structure ; palmitoleic acid ; pathogenesis
• 刊名：Acta Crystallographica Section F
• 出版年：2016
• 出版时间：September 2016
• 年：2016
• 卷：72
• 期：9
• 页码：726-731
• 全文大小：909K
• ISSN：1744-3091

文摘

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.