2i5l
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= cspB, cspA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= cspB, cspA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1csp|1CSP]], [[1csq|1CSQ]], [[2es2|2ES2]], [[2i5m|2I5M]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i5l OCA], [http://www.ebi.ac.uk/pdbsum/2i5l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i5l RCSB]</span> | ||
}} | }} | ||
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[[Category: oligonucleotide/oligosaccharide binding fold]] | [[Category: oligonucleotide/oligosaccharide binding fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:40:01 2008'' |
Revision as of 00:40, 31 March 2008
| |||||||
| , resolution 2.550Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | cspB, cspA (Bacillus subtilis) | ||||||
| Related: | 1CSP, 1CSQ, 2ES2, 2I5M
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Bacillus subtilis Cold Shock Protein variant Bs-CspB M1R/E3K/K65I
Overview
The bacterial cold shock proteins (Csp) are widely used as models for the experimental and computational analysis of protein stability. In a previous study, in vitro evolution was employed to identify strongly stabilizing mutations in Bs-CspB from Bacillus subtilis. The best variant found by this approach contained the mutations M1R, E3K and K65I, which raised the midpoint of thermal unfolding of Bs-CspB from 53.8 degrees C to 83.7 degrees C, and increased the Gibbs free energy of stabilization by 20.9 kJ mol(-1). Another selected variant with the two mutations A46K and S48R was stabilized by 11.1 kJ mol(-1). To elucidate the molecular basis of these stabilizations, we determined the crystal structures of these two Bs-CspB variants. The mutated residues are generally well ordered and provide additional stabilizing interactions, such as charge interactions, additional hydrogen bonds and improved side-chain packing. Several mutations improve the electrostatic interactions, either by the removal of unfavorable charges (E3K) or by compensating their destabilizing interactions (A46K, S48R). The stabilizing mutations are clustered at a contiguous surface area of Bs-CspB, which apparently is critically important for the stability of the beta-barrel structure but not well optimized in the wild-type protein.
About this Structure
2I5L is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Optimized variants of the cold shock protein from in vitro selection: structural basis of their high thermostability., Max KE, Wunderlich M, Roske Y, Schmid FX, Heinemann U, J Mol Biol. 2007 Jun 15;369(4):1087-97. Epub 2007 Apr 12. PMID:17481655
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