Probing the determinants of protein stability: comparison of class A beta-lactamases.


Abstract

Five class A beta-lactamases produced by various mesophilic bacterial species have been compared. Although closely related in primary and overall structures, these enzymes exhibit very different stabilities. In order to investigate the factors responsible for these differences, several features deduced from the amino acid composition and three-dimensional structures were studied for the five proteins. This analysis revealed that higher stability appeared to correlate with increased numbers of intramolecular hydrogen bonds and of salt bridges. By contrast, the global hydrophobicity of the protein seemed to play a relatively minor role. A strongly unfavourable balance between charged residues and the presence of a cis-peptide bond preceding a non-proline residue might also contribute to the particularly low stability of two of the enzymes. Study holds ProTherm entries: 7715, 7716, 7717 Extra Details: cis-peptide bond

Submission Details

ID: FyEc6Fkc

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Vanhove M;Houba S;b1motte-Brasseur J;Frère JM,Biochem. J. (1995) Probing the determinants of protein stability: comparison of class A beta-lactamases. PMID:8948443
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
1I2S 2001-02-12T00:00:00+0000 1.7 BETA-LACTAMASE FROM BACILLUS LICHENIFORMIS BS3
1I2W 2001-02-12T00:00:00+0000 1.7 BETA-LACTAMASE FROM BACILLUS LICHENIFORMIS BS3 COMPLEXED WITH CEFOXITIN
1MBL 1992-08-17T00:00:00+0000 2.0 A catalytically-impaired class A beta-lactamase: 2 Angstroms crystal structure and kinetics of the Bacillus licheniformis E166A mutant
1W7F 2004-09-01T00:00:00+0000 1.8 Crystal structure of the class A beta-lactamase BS3 inhibited with isocitrate
2BLM 1990-02-02T00:00:00+0000 2.0 BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION
2WK0 2009-06-03T00:00:00+0000 1.65 Crystal structure of the class A beta-lactamase BS3 inhibited by 6- beta-iodopenicillanate.
2Y91 2011-02-11T00:00:00+0000 2.0 Crystal structure of class A beta-lactamase from Bacillus licheniformis BS3 with clavulanic acid
3B3X 2007-10-23T00:00:00+0000 2.5 Crystal structure of class A beta-lactamase of Bacillus licheniformis BS3 with aminocitrate
3LY3 2010-02-26T00:00:00+0000 1.8 Crystal Structure of fluorophore-labeled Class A Beta-lactamase PenP
3LY4 2010-02-26T00:00:00+0000 1.8 Crystal Structure of fluorophore-labeled Class A -lactamase PenP-E166Cb in complex with penicillin G

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Beta-lactamase P00808 BLAC_BACLI