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PDBsum entry 1csp

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Transcription regulation PDB id
1csp
Contents
Protein chain
67 a.a.
Waters ×40

References listed in PDB file
Key reference
Title Universal nucleic acid-Binding domain revealed by crystal structure of the b. Subtilis major cold-Shock protein.
Authors H.Schindelin, M.A.Marahiel, U.Heinemann.
Ref. Nature, 1993, 364, 164-168.
PubMed id 8321288
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.
Secondary reference #1
Title Overproduction, Crystallization, And preliminary X-Ray diffraction studies of the major cold shock protein from bacillus subtilis, Cspb.
Authors H.Schindelin, M.Herrler, G.Willimsky, M.A.Marahiel, U.Heinemann.
Ref. Proteins, 1992, 14, 120-124.
PubMed id 1409560
Abstract
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