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XB-ART-22414
Nature 1993 Jul 08;3646433:169-71. doi: 10.1038/364169a0.
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Structure in solution of the major cold-shock protein from Bacillus subtilis.

Schnuchel A , Wiltscheck R , Czisch M , Herrler M , Willimsky G , Graumann P , Marahiel MA , Holak TA .


Abstract
The cold-shock domain (CSD) is found in many eukaryotic transcriptional factors and is responsible for the specific binding to DNA of a cis-element called the Y-box. The same domain exists in the sequence of the Xenopus RNA-binding proteins FRG Y1 and FRG Y2 (refs 1, 3). The major cold-shock proteins of Escherichia coli (CS7.4) and B. subtilis (CspB) have sequences that are more than 40 per cent identical to the cold-shock domain. We present here the three-dimensional structure of CspB determined by nuclear magnetic resonance spectroscopy. The 67-residue protein consists of an antiparallel five-stranded beta-barrel with strands connected by turns and loops. The structure resembles that of staphylococcal nuclease and the gene-5 single-stranded-DNA-binding protein. A three-stranded beta-sheet, which contains the conserved RNA-binding motif RNP1 as well as a motif similar to RNP2 in two neighbouring antiparallel beta-strands, has basic and aromatic residues at its surface which could serve as a binding site for single-stranded DNA. CspB binds to single-stranded DNA in gel retardation experiments.

PubMed ID: 8321289
Article link: Nature


Species referenced: Xenopus
Genes referenced: tgfbi ybx1 ybx2