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| - | [[Image:1c9o.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1c9o| PDB=1c9o | SCENE= }} | | {{STRUCTURE_1c9o| PDB=1c9o | SCENE= }} |
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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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| - | ==Overview==
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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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10736231}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10736231 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10736231}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Beta barrel]] | | [[Category: Beta barrel]] |
| | [[Category: Homodimer]] | | [[Category: Homodimer]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:30:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:24:50 2008'' |
Revision as of 17:24, 30 June 2008
Template:STRUCTURE 1c9o
CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP
Template:ABSTRACT PUBMED 10736231
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 Mon Jun 30 20:24:50 2008
