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
5TVY 2017-10-04 1.0 Computationally Designed Fentanyl Binder - Fen49
2Z79 2007-12-11 1.3 High resolution crystal structure of a glycoside hydrolase family 11 xylanase of Bacillus subtilis
2DCY 2006-02-07 1.4 Crystal structure of Bacillus subtilis family-11 xylanase
1XNB 1994-12-20 1.49 HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS
2BVV 1999-06-02 1.5 SUGAR RING DISTORTION IN THE GLYCOSYL-ENZYME INTERMEDIATE OF A FAMILY G/11 XYLANASE.
1C5H 2000-05-12 1.55 HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE
3VZK 2013-05-08 1.55 Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35E mutant
1HV0 2001-09-14 1.6 DISSECTING ELECTROSTATIC INTERACTIONS AND THE PH-DEPENDENT ACTIVITY OF A FAMILY 11 GLYCOSIDASE
1XNC 1994-12-20 1.6 THERMOSTABILIZATION OF THE BACILLUS CIRCULANS XYLANASE, BY THE INTRODUCTION OF DISULFIDE BONDS
3VZN 2013-05-08 1.67 Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35E mutant with Glu78 covalently bonded to 2-deoxy-2-fluoro-xylobiose
5TZO 2017-10-04 1.67 Computationally Designed Fentanyl Binder - Fen49*-Complex
1XXN 2005-10-18 1.7 Crystal structure of a mesophilic xylanase A from Bacillus subtilis 1A1
3VZO 2013-05-08 1.73 Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35H mutant with Glu78 covalently bonded to 2-deoxy-2-fluoro-xylobiose
5TVV 2017-10-04 1.79 Computationally Designed Fentanyl Binder - Fen49* Apo
2QZ3 2007-12-11 1.8 Crystal structure of a glycoside hydrolase family 11 xylanase from Bacillus subtilis in complex with xylotetraose
1BVV 1999-06-08 1.8 SUGAR RING DISTORTION IN THE GLYCOSYL-ENZYME INTERMEDIATE OF A FAMILY G/11 XYLANASE
1HV1 2001-09-14 1.8 DISSECTING ELECTROSTATIC INTERACTIONS AND THE PH-DEPENDENT ACTIVITY OF A FAMILY 11 GLYCOSIDASE
1C5I 2000-05-12 1.8 HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE
1BCX 1994-10-15 1.81 MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE
3EXU 2009-08-25 1.81 A glycoside hydrolase family 11 xylanase with an extended thumb region
3VZM 2013-05-08 1.86 Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) E172H mutant with Glu78 covalently bonded to 2-deoxy-2-fluoro-xylobiose
2DCZ 2006-02-07 1.9 Thermal Stabilization of Bacillus subtilis Family-11 Xylanase By Directed Evolution
3VZL 2013-05-08 2.0 Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35H mutant
2B45 2006-09-19 2.0 Crystal structure of an engineered uninhibited Bacillus subtilis xylanase in free state
1AXK 1999-05-11 2.1 ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1
5K9Y 2017-04-12 2.2 Crystal structure of a thermophilic xylanase A from Bacillus subtilis 1A1 quadruple mutant Q7H/G13R/S22P/S179C
2B46 2006-09-19 2.21 Crystal structure of an engineered uninhibited Bacillus subtilis xylanase in substrate bound state
3HD8 2009-06-30 2.39 Crystal structure of the Triticum aestivum xylanase inhibitor-IIA in complex with bacillus subtilis xylanase
3VZJ 2013-05-08 2.41 Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) E172H mutant
2B42 2006-09-19 2.5 Crystal structure of the Triticum xylanse inhibitor-I in complex with bacillus subtilis xylanase
3LB9 2010-03-23 3.0 Crystal structure of the B. circulans cpA123 circular permutant

Relevant UniProtKB Entries

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