H. Schindelin et al., CRYSTAL-STRUCTURE OF CSPA, THE MAJOR COLD SHOCK PROTEIN OF ESCHERICHIA-COLI, Proceedings of the National Academy of Sciences of the United Statesof America, 91(11), 1994, pp. 5119-5123
The major cold shock protein of Escherichia coli, CspA, produced upon
a rapid downshift in growth temperature, is involved in the transcript
ional regulation of at least two genes. The protein shares high homolo
gy 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-Ang
strom resolution and refined to R = 0.187. CspA is composed of five an
tiparallel beta-strands forming a closed five-stranded beta-barrel. Th
e 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-Angstrom resolution. However, in contrast to CspB,
no dimer is formed in the crystal. The surface of CspA is characteris
tic for a protein interacting with single-stranded nucleic acids. Due
to the high homology of the bacterial cold shock proteins with the Y-b
ox factors, E. coli CspA and B. subtilis CspB define a structural fram
ework for the common cold shock domain.