Format

Send to

Choose Destination
Acta Crystallogr F Struct Biol Commun. 2016 Sep;72(Pt 9):726-31. doi: 10.1107/S2053230X1601298X. Epub 2016 Aug 26.

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

Author information

1
Department of Molecular Bioscience, The University of Kansas, 8031 Haworth, 1200 Sunnyside Avenue, Lawrence, KS 66045, USA.
2
Protein Structure Laboratory, Shankel Structural Biology Center, The University of Kansas, 2034 Becker Drive, Lawrence, KS 66047, USA.
3
IMCA-CAT, Hauptman-Woodward Medical Research Institute, 9700 South Cass Avenue, Building 435A, Argonne, IL 60439, USA.

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.

KEYWORDS:

AraC; ToxT; Vibrio cholerae; crystal structure; palmitoleic acid; pathogenesis

PMID:
27599865
PMCID:
PMC5012214
DOI:
10.1107/S2053230X1601298X
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for International Union of Crystallography Icon for PubMed Central
Loading ...
Support Center