1MJC

CRYSTAL STRUCTURE OF CSPA, THE MAJOR COLD SHOCK PROTEIN OF ESCHERICHIA COLI

Summary for 1MJC

• Entry DOI: 10.2210/pdb1mjc/pdb
• Descriptor: MAJOR COLD-SHOCK PROTEIN 7.4 (2 entities in total)
• Functional Keywords: transcription regulation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 7280.06

Authors

Schindelin, H.,Heinemann, U. (deposition date: 1994-03-18, release date: 1994-06-22, Last modification date: 2024-02-14)

Primary citation

Schindelin, H.,Jiang, W.,Inouye, M.,Heinemann, U.
Crystal structure of CspA, the major cold shock protein of Escherichia coli.
Proc.Natl.Acad.Sci.USA, 91:5119-5123, 1994

PubMed 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.

PubMed: 8197194
DOI: 10.1073/pnas.91.11.5119

Experimental method

X-RAY DIFFRACTION (2 Å)