1csp

<table><tr><td colspan='2'>[[1csp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSP FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1csp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csp OCA], [https://pdbe.org/1csp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1csp RCSB], [https://www.ebi.ac.uk/pdbsum/1csp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1csp ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/CSPB_BACSU CSPB_BACSU]] Binds to the pentamer sequences ATTGG and CCAAT with highest affinity in single-stranded DNA, and also to other sequences. Has greater affinity for ATTGG than CCAAT. Can act as transcriptional activator of cold shock genes by recognizing putative ATTGG-box elements present in promoter regions of genes induced under cold shock conditions.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:8321288</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Heinemann, U]]

[[Category: Schindelin, H]]

[[Category: Transcription regulation]]