Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds.


Abstract

The introduction of disulfide bonds has been used as a strategy to enhance the stability of Bacillus circulans xylanase. The transition temperature of the S100C/N148C (DS1), V98C/A152C (DS2), and A1GC/G187,C188 (cXl) in comparison to the wild type was increased by 5.0, 4.1 and 3.8 degrees C, respectively. Interestingly, a combination of two disulfide bonds of DS1 and cXl (cDS1, circular disulfide 1) led to a 12 degrees C increase in the transition temperature. Importantly, an increase in the melting point and DeltaDeltaG values of the cDS1 mutant was cooperative. These results suggest that the mechanism of stabilization by disulfide bonds under irreversible denaturation condition is achieved through: (1) a change in the rate-limiting step on the denaturation pathway; (2) destabilizing the unfolded state without affecting the relative rate constants on the denaturation pathway (like cXl mutant); and (3) or combination of the two (cDS1 mutant). Study holds ProTherm entries: 22319, 22320, 22321, 22322, 22323, 22324, 22325, 22326, 22327, 22328, 22329, 22330, 22331, 22332, 22333, 22334, 22335, 22336, 22337, 22338, 22339, 22340, 22341, 22342, 22343, 22344 Extra Details: data were obtained with the scanning rate of 57 degrees/h Xylanase; Stabilization; Disulfide bond

Submission Details

ID: RUFkPFGm3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:53 p.m.

Version: 1

Publication Details
Davoodi J;Wakarchuk WW;Carey PR;Surewicz WK,Biophys. Chem. (2007) Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds. PMID:17141401
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1AXK 1997-10-16T00:00:00+0000 2.1 ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1
1XXN 2004-11-07T00:00:00+0000 1.7 Crystal structure of a mesophilic xylanase A from Bacillus subtilis 1A1
2B42 2005-09-22T00:00:00+0000 2.5 Crystal structure of the Triticum xylanse inhibitor-I in complex with bacillus subtilis xylanase
2B45 2005-09-22T00:00:00+0000 2.0 Crystal structure of an engineered uninhibited Bacillus subtilis xylanase in free state
2B46 2005-09-22T00:00:00+0000 2.21 Crystal structure of an engineered uninhibited Bacillus subtilis xylanase in substrate bound state
2DCY 2006-01-18T00:00:00+0000 1.4 Crystal structure of Bacillus subtilis family-11 xylanase
2DCZ 2006-01-18T00:00:00+0000 1.9 Thermal Stabilization of Bacillus subtilis Family-11 Xylanase By Directed Evolution
2QZ3 2007-08-16T00:00:00+0000 1.8 Crystal structure of a glycoside hydrolase family 11 xylanase from Bacillus subtilis in complex with xylotetraose
2Z79 2007-08-16T00:00:00+0000 1.3 High resolution crystal structure of a glycoside hydrolase family 11 xylanase of Bacillus subtilis
3EXU 2008-10-17T00:00:00+0000 1.81 A glycoside hydrolase family 11 xylanase with an extended thumb region

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Endo-1,4-beta-xylanase P09850 XYNA_BACCI
99.5 Endo-1,4-beta-xylanase P18429 XYNA_BACSU