Dissemin is shutting down on January 1st, 2025

Published in

International Union of Crystallography, Acta Crystallographica Section F: Structural Biology Communications, 9(72), p. 726-731, 2016

DOI: 10.1107/s2053230x1601298x

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 2016 by Jiaqin Li, Graham Wehmeyer ORCID, Scott Lovell, Kevin P. Battaile, Susan M. Egan ORCID
This paper is available in a repository.
This paper is available in a repository.

Full text: Download

Green circle
Preprint: archiving allowed
Green circle
Postprint: archiving allowed
Green circle
Published version: archiving allowed
Data provided by SHERPA/RoMEO

Abstract

ToxT is an AraC-family transcriptional activator protein that controls the expression of key virulence factors inVibrio 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 thetcppromoter. 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.