1.65 Å resolution structure of the AraC‐family transcriptional activator ToxT from Vibrio cholerae. Issue 9 (8th September 2016)

• Record Type: Journal Article
• Authors: Li, Jiaqin; Wehmeyer, Graham; Lovell, Scott; Battaile, Kevin P.; Egan, Susan M.
• Is Part Of: Acta crystallographica. Volume 72:Issue 9(2016:Sep.)
• Page Start: 726
• Page End: 731
• Publication Date: 2016-09-08
• Subjects: AraC -- ToxT -- Vibrio cholerae -- crystal structure -- palmitoleic acid -- pathogenesis; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1601298X
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : A crystal structure of ToxT at 1.65 Å resolution with a similar overall structure to the previously determined structure is reported. A region that extends from Asp101 to Glu110, which can influence ToxT activity but was disordered in the previous structure, can be traced entirely in the current structure. 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 entry3gbg ). 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.