1csp
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(New page: 200px<br /><applet load="1csp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1csp, resolution 2.45Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 10:36, 20 November 2007
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CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN
Overview
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.
About this Structure
1CSP is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein., Schindelin H, Marahiel MA, Heinemann U, Nature. 1993 Jul 8;364(6433):164-8. PMID:8321288
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