This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2i5l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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

Image: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

Retrieved from "http://52.214.119.220/wiki/index.php/2i5l"
Personal tools