1CSP

CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN

Summary for 1CSP

• Entry DOI: 10.2210/pdb1csp/pdb
• Descriptor: COLD SHOCK PROTEIN B(CSPB) (2 entities in total)
• Functional Keywords: transcription regulation
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm, nucleoid : P32081
• Total number of polymer chains: 1
• Total formula weight: 7372.13

Authors

Schindelin, H.,Heinemann, U. (deposition date: 1993-05-12, release date: 1995-05-12, Last modification date: 2024-02-07)

Primary citation

Schindelin, H.,Marahiel, M.A.,Heinemann, U.
Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein.
Nature, 364:164-168, 1993

PubMed Abstract: The cold-shock response in both Escherichia coli and Bacillus subtilis is induced by an abrupt downshift in growth temperature. It leads to the increased production of the major cold-shock proteins, CS7.4 and CspB, respectively. CS7.4 is a transcriptional activator of two genes. CS7.4 and CspB share 43 per cent sequence identity with the nucleic acid-binding domain of the eukaryotic gene-regulatory Y-box factors. This cold-shock domain is conserved from bacteria to man and contains the RNA-binding RNP1 sequence motif. As a prototype of the cold-shock domain, the structure of CspB has been determined here from two crystal forms. In both, CspB is present as an antiparallel five-stranded beta-barrel. Three consecutive beta-strands, the central one containing the RNP1 motif, create a surface rich in aromatic and basic residues that are presumably involved in nucleic acid binding. Preferential binding of CspB to single-stranded DNA is observed in gel retardation experiments.

PubMed: 8321288
DOI: 10.1038/364164a0

Experimental method

X-RAY DIFFRACTION (2.45 Å)