Open AccessExpression and crystallization of SeDsbA, SeDsbL and SeSrgA from Salmonella enterica serovar Typhimurium
Author(s) -
Jarrott R.,
Shouldice S. R.,
Gunčar G.,
Totsika M.,
Schembri M. A.,
Heras B.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110011942
Subject(s) - salmonella enterica , virulence , microbiology and biotechnology , bacteria , escherichia coli , salmonella , biology , oxidative folding , protein folding , chemistry , enzyme , biochemistry , gene , protein disulfide isomerase , genetics
Pathogens require protein‐folding enzymes to produce functional virulence determinants. These foldases include the Dsb family of proteins, which catalyze oxidative folding in bacteria. Bacterial disulfide catalytic processes have been well characterized in Escherichia coli K‐12 and these mechanisms have been extrapolated to other organisms. However, recent research indicates that the K‐12 complement of Dsb proteins is not common to all bacteria. Importantly, many pathogenic bacteria have an extended arsenal of Dsb catalysts that is linked to their virulence. To help to elucidate the process of oxidative folding in pathogens containing a wide repertoire of Dsb proteins, Salmonella enterica serovar Typhimurium has been focused on. This Gram‐negative bacterium contains three DsbA proteins: SeDsbA, SeDsbL and SeSrgA. Here, the expression, purification, crystallization and preliminary diffraction analysis of these three proteins are reported. SeDsbA, SeDsbL and SeSrgA crystals diffracted to resolution limits of 1.55, 1.57 and 2.6 Å and belonged to space groups P 2 1 , P 2 1 2 1 2 and C 2, respectively.