![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
| Item Type: | Article |
|---|---|
| Title: | Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein |
| Creators Name: | Schindelin, H., Marahiel, M.A. and Heinemann, U. |
| 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. |
| Keywords: | Amino Acid Sequence, Bacillus subtilis, Bacterial Proteins, Base Sequence, Binding Sites, Crystallography, DNA-Binding Proteins, Molecular Models, Molecular Sequence Data, Secondary Protein Structure, Tertiary Protein Structure, RNA-Binding Proteins |
| Source: | Nature |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Volume: | 364 |
| Number: | 6433 |
| Page Range: | 164-168 |
| Date: | 8 July 1993 |
| Official Publication: | https://doi.org/10.1038/364164a0 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
