1csp
From Proteopedia
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- | [[Image:1csp.gif|left|200px]] | + | [[Image:1csp.gif|left|200px]] |
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- | '''CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN''' | + | {{Structure |
+ | |PDB= 1csp |SIZE=350|CAPTION= <scene name='initialview01'>1csp</scene>, resolution 2.45Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1CSP is a [ | + | 1CSP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSP OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8321288 8321288] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:29 2008'' |
Revision as of 08:28, 20 March 2008
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, resolution 2.45Å | |||||||
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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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