Crystal structure of CspA, the major cold shock protein of Escherichia coli

Hermann Schindelin, Weining Jiang, Masayori Inouye, Udo Heinemann

Research output: Contribution to journalArticlepeer-review

293 Scopus citations

Abstract

The major cold shock protein of Escherichia coli, CspA, produced upon a rapid downshift in growth temperature, is involved in the transcriptional regulation of at least two genes. The protein shares high homology with the nucleic acid-binding domain of the Y-box factors, a family of eukaryotic proteins involved in transcriptional and translational regulation. The crystal structure of CspA has been determined at 2-Å resolution and refined to R = 0.187. CspA is composed of five antiparallel β-strands forming a closed five-stranded β-barrel. The three-dimensional structure of CspA is similar to that of the major cold shock protein of Bacillus subtilis, CspB, which has recently been determined at 2.45-Å resolution. However, in contrast to CspB, no dimer is formed in the crystal. The surface of CspA is characteristic for a protein interacting with single-stranded nucleic acids. Due to the high homology of the bacterial cold shock proteins with the Y-box factors, E. coli CspA and B. subtilis CspB define a structural framework for the common cold shock domain.

Original languageEnglish (US)
Pages (from-to)5119-5123
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number11
DOIs
StatePublished - May 24 1994

All Science Journal Classification (ASJC) codes

  • General

Keywords

  • Y-box factors
  • cold shock domain
  • nucleic acid binding
  • x-ray crystallography

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