1csp
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1csp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csp OCA], [http://www.ebi.ac.uk/pdbsum/1csp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1csp RCSB]</span> | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:27:47 2008'' |
Revision as of 16:27, 30 March 2008
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| , resolution 2.45Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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