2i5l: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2i5l.jpg|left|200px]]
{{Seed}}
[[Image:2i5l.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2i5l|  PDB=2i5l  |  SCENE=  }}  
{{STRUCTURE_2i5l|  PDB=2i5l  |  SCENE=  }}  


'''Crystal structure of Bacillus subtilis Cold Shock Protein variant Bs-CspB M1R/E3K/K65I'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_17481655}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17481655 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17481655}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Expression regulator]]
[[Category: Expression regulator]]
[[Category: Oligonucleotide/oligosaccharide binding fold]]
[[Category: Oligonucleotide/oligosaccharide binding fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:06:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:58:33 2008''

Revision as of 21:58, 5 July 2008

File:2i5l.png

Template:STRUCTURE 2i5l

Crystal structure of Bacillus subtilis Cold Shock Protein variant Bs-CspB M1R/E3K/K65I

Template:ABSTRACT PUBMED 17481655

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 Sun Jul 6 00:58:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA