15N, 13C and 1H backbone resonance assignments of an artificially engineered TEM-1/PSE-4 class A ß-lactamase chimera and its deconvoluted mutant.
Biomol NMR Assign
; 10(1): 93-9, 2016 Apr.
Article
em En
| MEDLINE
| ID: mdl-26386961
ABSTRACT
The widespread use of ß-lactam antibiotics has given rise to a dramatic increase in clinically-relevant ß-lactamases. Understanding the structure/function relation in these variants is essential to better address the ever-growing incidence of antibiotic resistance. We previously reported the backbone resonance assignments of a chimeric protein constituted of segments of the class A ß-lactamases TEM-1 and PSE-4 (Morin et al. in Biomol NMR Assign 4127-130, 2010. doi 10.1007/s12104-010-9227-8 ). That chimera, cTEM17m, held 17 amino acid substitutions relative to TEM-1 ß-lactamase, resulting in a well-folded and fully functional protein with increased dynamics. Here we report the (1)H, (13)C and (15)N backbone resonance assignments of chimera cTEM-19m, which includes 19 substitutions and exhibits increased active-site perturbation, as well as one of its deconvoluted variants, as the first step in the analysis of their dynamic behaviours.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Beta-Lactamases
/
Proteínas Recombinantes
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Engenharia de Proteínas
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Ressonância Magnética Nuclear Biomolecular
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Proteínas Mutantes
Idioma:
En
Revista:
Biomol NMR Assign
Assunto da revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Canadá