1c9o
From Proteopedia
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|PDB= 1c9o |SIZE=350|CAPTION= <scene name='initialview01'>1c9o</scene>, resolution 1.17Å | |PDB= 1c9o |SIZE=350|CAPTION= <scene name='initialview01'>1c9o</scene>, resolution 1.17Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1csp|1CSP]], [[1mjc|1MJC]] | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1c9o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c9o RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Perl, D.]] | [[Category: Perl, D.]] | ||
[[Category: Schmid, F X.]] | [[Category: Schmid, F X.]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: TRS]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: homodimer]] | [[Category: homodimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:27 2008'' |
Revision as of 16:17, 30 March 2008
| |||||||
| , resolution 1.17Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1CSP, 1MJC
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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