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1c9o

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[[Image:1c9o.jpg|left|200px]]<br /><applet load="1c9o" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1c9o, resolution 1.17&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP==
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The bacterial cold shock proteins are small compact beta-barrel proteins without disulfide bonds, cis-proline residues or tightly bound cofactors. Bc-Csp, the cold shock protein from the thermophile Bacillus caldolyticus shows a twofold increase in the free energy of stabilization relative to its homolog Bs-CspB from the mesophile Bacillus subtilis, although the two proteins differ by only 12 out of 67 amino acid residues. This pair of cold shock proteins thus represents a good system to study the atomic determinants of protein thermostability. Bs-CspB and Bc-Csp both unfold reversibly in cooperative transitions with T(M) values of 49.0 degrees C and 77.3 degrees C, respectively, at pH 7.0. Addition of 0.5 M salt stabilizes Bs-CspB but destabilizes Bc-Csp. To understand these differences at the structural level, the crystal structure of Bc-Csp was determined at 1.17 A resolution and refined to R=12.5% (R(free)=17.9%). The molecular structures of Bc-Csp and Bs-CspB are virtually identical in the central beta-sheet and in the binding region for nucleic acids. Significant differences are found in the distribution of surface charges including a sodium ion binding site present in Bc-Csp, which was not observed in the crystal structure of the Bs-CspB. Electrostatic interactions are overall favorable for Bc-Csp, but unfavorable for Bs-CspB. They provide the major source for the increased thermostability of Bc-Csp. This can be explained based on the atomic-resolution crystal structure of Bc-Csp. It identifies a number of potentially stabilizing ionic interactions including a cation-binding site and reveals significant changes in the electrostatic surface potential.
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<StructureSection load='1c9o' size='340' side='right'caption='[[1c9o]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1c9o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_caldolyticus Bacillus caldolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9O FirstGlance]. <br>
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1C9O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_caldolyticus Bacillus caldolyticus] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9O 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]] 1.17&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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==Reference==
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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=1c9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9o OCA], [https://pdbe.org/1c9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9o RCSB], [https://www.ebi.ac.uk/pdbsum/1c9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9o ProSAT]</span></td></tr>
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Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein., Mueller U, Perl D, Schmid FX, Heinemann U, J Mol Biol. 2000 Apr 7;297(4):975-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10736231 10736231]
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</table>
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[[Category: Bacillus caldolyticus]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/CSPB_BACCL CSPB_BACCL] Affects cell viability at low temperatures.
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[[Category: Heinemann, U.]]
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== Evolutionary Conservation ==
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[[Category: Mueller, U.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Perl, D.]]
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Check<jmol>
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[[Category: Schmid, F X.]]
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<jmolCheckbox>
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[[Category: NA]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c9o_consurf.spt"</scriptWhenChecked>
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[[Category: TRS]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: beta barrel]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: homodimer]]
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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=1c9o ConSurf].
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:53 2008''
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Heinemann U]]
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[[Category: Mueller U]]
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[[Category: Perl D]]
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[[Category: Schmid FX]]

Current revision

CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP

PDB ID 1c9o

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