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Cited by 344

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

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Schindelin, H, Jiang, W, Inouye, M, Heinemann, U·1994·Proceedings of the National Academy of Sciences

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.

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Crossref · 10.1073/pnas.91.11.5119

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Metadata

Authors
Schindelin, H., Jiang, W., Inouye, M., & Heinemann, U.
Venue
Proceedings of the National Academy of Sciences
Published
1994-05-24
Volume
91
Issue
11
Pages
5119-5123
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1988299779
Cited by
344
References
1
FWCI
5.64
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Crystal structure of CspA, the major cold shock protein of Escherichia coli. https://app.cochat.ai/papers/10.1073/pnas.91.11.5119
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Schindelin, H., Jiang, W., Inouye, M., & Heinemann, U. (1994). Crystal structure of CspA, the major cold shock protein of Escherichia coli. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.11.5119

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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