Crystal structure of CspA, the major cold shock protein of Escherichia coli.
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.
Schindelin
H
H
Forschungsgruppe Kristallographie, Max-Delbrúck-Centrum für Molekulare Medizin, Berlin, Germany.
Jiang
W
W
Inouye
M
M
Heinemann
U
U
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial; D004926:Escherichia coli / Q000737:chemistry*; D006801:Humans; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D009841:Oligonucleotides / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry*
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D009841:Oligonucleotides; D009844:Oligosaccharides; D014157:Transcription Factors; C062260:cold shock protein CS7.4, Bacteria; C077188:cold-shock protein CspB, Bacteria