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'''CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP''' | '''CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP''' | ||
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[[Category: Perl, D.]] | [[Category: Perl, D.]] | ||
[[Category: Schmid, F X.]] | [[Category: Schmid, F X.]] | ||
[[Category: | [[Category: Beta barrel]] | ||
[[Category: | [[Category: Homodimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:30:03 2008'' | |||
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Revision as of 09:30, 2 May 2008
CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP
Overview
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.
About this Structure
1C9O is a Single protein structure of sequence from Bacillus caldolyticus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 12:30:03 2008
