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 2.45&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1csp.gif|left|200px]]<br /><applet load="1csp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1csp, resolution 2.45&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN==
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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.
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<StructureSection load='1csp' size='340' side='right'caption='[[1csp]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1csp]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSP FirstGlance]. <br>
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1CSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CSP OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<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>
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==Reference==
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</table>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8321288 8321288]
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== Function ==
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cs/1csp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1csp ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Heinemann, U.]]
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[[Category: Heinemann U]]
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[[Category: Schindelin, H.]]
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[[Category: Schindelin H]]
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[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:43:45 2007''
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Current revision

CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN

PDB ID 1csp

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