3I2Z

Structure of cold shock protein E from Salmonella typhimurium

Summary for 3I2Z

• Entry DOI: 10.2210/pdb3i2z/pdb
• Related: 1C9O 1CSP 1MJC 2ES2 2HAX
• Descriptor: RNA chaperone, negative regulator of cspA transcription (2 entities in total)
• Functional Keywords: beta barrel, dna binding protein/transcription, cytoplasm, gene regulation
• Biological source: Salmonella typhimurium
• Cellular location: Cytoplasm (By similarity): Q7CQZ5
• Total number of polymer chains: 2
• Total formula weight: 15371.19

Authors

Morgan, H.P.,McNae, I.,Wear, M.A.,Gallagher, M.,Walkinshaw, M.D. (deposition date: 2009-06-30, release date: 2009-12-22, Last modification date: 2023-11-01)

Primary citation

Morgan, H.P.,Wear, M.A.,McNae, I.,Gallagher, M.P.,Walkinshaw, M.D.
Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimurium
Acta Crystallogr.,Sect.F, 65:1240-1245, 2009

PubMed 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.

PubMed: 20054119
DOI: 10.1107/S1744309109033788

Experimental method

X-RAY DIFFRACTION (1.1 Å)