ArticleProceedings of the National Academy of Sciences of the United States of America1994
Crystal structure of CspA, the major cold shock protein of Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.
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Who cites it
124 citing papers in PubMed, 347 citations in OpenAlex.
- The Role of Cold Shock Protein (CSP) Gene Family in Yak (Bos grunniens) for High-Altitude Adaptation: Genome-Wide Identification and Analysis.Animal genetics · 2026Article
- Knowledge Distillation of a Protein Language Model Yields a Foundational Implicit Solvent Model.Journal of chemical theory and computation · 2026Article
- Multiscale Neural Network Potential with Anisotropic Message Passing for the Fast and Accurate Simulation of Protein Dynamics and Enzymatic Reactions.Journal of the American Chemical Society · 2026Article
- Knowledge Distillation of a Protein Language Model Yields a Foundational Implicit Solvent Model.ArXiv · 2026Article
- Methionine Oxidation Footprinting in Intact Proteins (MOFIP) Using Top-Down Proteomics.Proteomics · 2025Article
- Genetic Characterization and Symbiotic Performance of Soybean Rhizobia Under Cold and Water-Deficient Conditions in Poland.Plants (Basel, Switzerland) · 2025Article
- Temporal changes in cold-inducible and uncharacterized Csps under heat and oxidative stress signify a role in bacterial stress response and adaptation.Archives of microbiology · 2025Article
- An internal loop region is responsible for inherent target specificity of bacterial cold-shock proteins.RNA (New York, N.Y.) · 2024Article
- Traversing DNA-Protein Interactions Between Mesophilic and Thermophilic Bacteria: Implications from Their Cold Shock Response.Molecular biotechnology · 2024Article
- From Stress Tolerance to Virulence: Recognizing the Roles of Csps in Pathogenicity and Food Contamination.Pathogens (Basel, Switzerland) · 2024Review
- A high-throughput search for intracellular factors that affect RNA folding identifiesRNA biology · 2024Article
- Structural and biochemical insights into the bacteriophage PlyGRCS endolysin targeting methicillin-resistant Staphylococcus aureus (MRSA) and serendipitous discovery of its interaction with a cold shock protein C (CspC).Protein science : a publication of the Protein Society · 2023Article
- NMR detection and conformational dependence of two, three, and four-bond isotope shifts due to deuteration of backbone amides.Journal of biomolecular NMR · 2023Article
- Article
- Phylogenetic Association and Genetic Factors in Cold Stress Tolerance in Campylobacter jejuni.Microbiology spectrum · 2022Article
- Article
- Assessing the Role of Cold-Shock Protein C: a Novel Regulator of Acinetobacter baumannii Biofilm Formation and Virulence.Infection and immunity · 2022Article
- A switch from α-helical to β-strand conformation during co-translational protein folding.The EMBO journal · 2022Article
- A cold shock protein promotes high-temperature microbial growth through binding to diverse RNA species.Cell discovery · 2021Article
- Review
64 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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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