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

Item Type:Article
Title:Crystal structure of CspA, the major cold shock protein of Escherichia coli
Creators Name:Schindelin, H., Jiang, W., Inouye, M. and Heinemann, U.
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-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.
Keywords:Amino Acid Sequence, Amino Acid Sequence Homology, Bacterial DNA, Bacterial Proteins, Base Sequence, Escherichia Coli, Isoelectric Point, Molecular Sequence Data, Oligonucleotides, Oligosaccharides, Protein Conformation, Transcription Factors, X-Ray Crystallography, Animals
Source:Proceedings of the National Academy of Sciences of the United States of America
Publisher:National Academy of Sciences
Page Range:5119-5123
Date:24 May 1994
Official Publication:http://www.pnas.org/content/91/11/5119.abstract
PubMed:View item in PubMed

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