Your browser doesn't support javascript.
loading
1.65 Šresolution structure of the AraC-family transcriptional activator ToxT from Vibrio cholerae.
Li, Jiaqin; Wehmeyer, Graham; Lovell, Scott; Battaile, Kevin P; Egan, Susan M.
Afiliación
  • Li J; Department of Molecular Bioscience, The University of Kansas, 8031 Haworth, 1200 Sunnyside Avenue, Lawrence, KS 66045, USA.
  • Wehmeyer G; Department of Molecular Bioscience, The University of Kansas, 8031 Haworth, 1200 Sunnyside Avenue, Lawrence, KS 66045, USA.
  • Lovell S; Protein Structure Laboratory, Shankel Structural Biology Center, The University of Kansas, 2034 Becker Drive, Lawrence, KS 66047, USA.
  • Battaile KP; IMCA-CAT, Hauptman-Woodward Medical Research Institute, 9700 South Cass Avenue, Building 435A, Argonne, IL 60439, USA.
  • Egan SM; Department of Molecular Bioscience, The University of Kansas, 8031 Haworth, 1200 Sunnyside Avenue, Lawrence, KS 66045, USA.
Acta Crystallogr F Struct Biol Commun ; 72(Pt 9): 726-31, 2016 09.
Article en En | MEDLINE | ID: mdl-27599865
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 Šresolution (PDB entry 3gbg). In this study, a crystal structure of ToxT at 1.65 Šresolution 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.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Factores de Transcripción / Vibrio cholerae / Proteínas Recombinantes de Fusión / Ácido Aspártico / Ácido Glutámico Tipo de estudio: Prognostic_studies Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Factores de Transcripción / Vibrio cholerae / Proteínas Recombinantes de Fusión / Ácido Aspártico / Ácido Glutámico Tipo de estudio: Prognostic_studies Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos