1mjc

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CRYSTAL STRUCTURE OF CSPA, THE MAJOR COLD SHOCK PROTEIN OF ESCHERICHIA COLI

Overview

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-A, resolution and refined to R = 0.187. CspA is composed of five antiparallel, beta-strands forming a closed five-stranded beta-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-A 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.

About this Structure

1MJC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of CspA, the major cold shock protein of Escherichia coli., Schindelin H, Jiang W, Inouye M, Heinemann U, Proc Natl Acad Sci U S A. 1994 May 24;91(11):5119-23. PMID:8197194

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