학술논문
Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimurium
Document Type
Academic Journal
Source
Acta Crystallographica Section F. Dec, 2009, Vol. 65 Issue 12, p1240, 6 p.
Subject
Language
English
ISSN
1744-3091
Abstract
To authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1107/S1744309109033788 Byline: Hugh P. Morgan, Martin A. Wear, Iain McNae, Maurice P. Gallagher, Malcolm D. Walkinshaw Keywords: cold-shock proteins; Salmonella typhimurium Abstract: 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: StCspA-E and StCspH. The crystal structure of cold-shock protein E from S. typhimurium (StCspE) has been determined at 1.1 A 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 [beta]-strands forming a classic OB fold/five-stranded [beta]-barrel. This first structure of a CSP from S. typhimurium provides new insight into the cold-shock response of this bacterium. Author Affiliation: (a)Centre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, Scotland Article History: Received 3 July 2009, accepted 24 August 2009 Article note: Malcolm D. Walkinshaw, e-mail: m.walkinshaw@ed.ac.uk