1c9o

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spinqualitylabelsall models 1c9o, resolution 1.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with NA and TRS as ligands. 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

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