1c9o

<table><tr><td colspan='2'>[[1c9o]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C9O FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1csp|1csp]], [[1mjc|1mjc]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9o OCA], [http://pdbe.org/1c9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c9o RCSB], [http://www.ebi.ac.uk/pdbsum/1c9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9o ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CSPB_BACCL CSPB_BACCL]] Affects cell viability at low temperatures.

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== Publication Abstract from PubMed ==

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.

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:10736231<ref>PMID:10736231</ref>

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

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== References ==

<references/>

[[Category: Bacillus caldolyticus]]

[[Category: Heinemann, U]]

[[Category: Mueller, U]]

[[Category: Perl, D]]

[[Category: Schmid, F X]]

[[Category: Transcription]]