2i5l
From Proteopedia
(New page: 200px<br /><applet load="2i5l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i5l, resolution 2.550Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2i5l.jpg|left|200px]]<br /><applet load="2i5l" size=" | + | [[Image:2i5l.jpg|left|200px]]<br /><applet load="2i5l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2i5l, resolution 2.550Å" /> | caption="2i5l, resolution 2.550Å" /> | ||
'''Crystal structure of Bacillus subtilis Cold Shock Protein variant Bs-CspB M1R/E3K/K65I'''<br /> | '''Crystal structure of Bacillus subtilis Cold Shock Protein variant Bs-CspB M1R/E3K/K65I'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2I5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 2I5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I5L OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 21: | ||
[[Category: oligonucleotide/oligosaccharide binding fold]] | [[Category: oligonucleotide/oligosaccharide binding fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:52:48 2008'' |
Revision as of 12:52, 23 January 2008
|
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
Page seeded by OCA on Wed Jan 23 14:52:48 2008
