Open AccessCrystallization and X‐ray structure of cold‐shock protein E from Salmonella typhimurium
Author(s) -
Morgan Hugh P.,
Wear Martin A.,
McNae Iain,
Gallagher Maurice P.,
Walkinshaw Malcolm D.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109033788
Subject(s) - cold shock domain , salmonella , antiparallel (mathematics) , escherichia coli , bacillus subtilis , crystallization , biology , microbiology and biotechnology , bacteria , chemistry , biochemistry , genetics , physics , rna , gene , organic chemistry , quantum mechanics , magnetic field
In prokaryotic organisms, cold shock triggers the production of a small highly conserved family of cold‐shock proteins (CSPs). CSPs have been well studied structurally and functionally in Escherichia coli and Bacillus subtilis , but Salmonella typhimurium CSPs remain relatively uncharacterized. In S. typhimurium , six homologous CSPs have been identified: St CspA–E and St CspH. The crystal structure of cold‐shock protein E from S. typhimurium ( St CspE) has been determined at 1.1 Å resolution and has an R factor of 0.203 after refinement. The three‐dimensional structure is similar to those of previously determined CSPs and is composed of five antiparallel β‐strands forming a classic OB fold/five‐stranded β‐barrel. This first structure of a CSP from S. typhimurium provides new insight into the cold‐shock response of this bacterium.