1NMG

MAJOR COLD-SHOCK PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1NMG

• Entry DOI: 10.2210/pdb1nmg/pdb
• Descriptor: MAJOR COLD-SHOCK PROTEIN (1 entity in total)
• Functional Keywords: cold shock protein, transcription regulation
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm, nucleoid : P32081
• Total number of polymer chains: 1
• Total formula weight: 7372.13

Authors

Schnuchel, A.,Holak, T.A. (deposition date: 1996-02-05, release date: 1996-07-11, Last modification date: 2024-05-01)

Primary citation

Schnuchel, A.,Wiltscheck, R.,Czisch, M.,Herrler, M.,Willimsky, G.,Graumann, P.,Marahiel, M.A.,Holak, T.A.
Structure in solution of the major cold-shock protein from Bacillus subtilis.
Nature, 364:169-171, 1993

PubMed 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: 8321289
DOI: 10.1038/364169a0

Experimental method

SOLUTION NMR