Gobeil, Sophie; Gagné, Donald; Doucet, Nicolas 
ORCID: https://orcid.org/0000-0002-1952-9380 et Pelletier, Joelle N.
(2016).
15N, 13C and 1H backbone resonance assignments of an artificially engineered TEM-1/PSE-4 class A β-lactamase chimera and its deconvoluted mutant
Biomolecular NMR Assignments
, vol. 10
, nº 1.
pp. 93-99.
DOI: 10.1007/s12104-015-9645-8.
Résumé
The widespread use of β-lactam antibiotics has given rise to a dramatic increase in clinically-relevant β-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 β-lactamases TEM-1 and PSE-4 (Morin et al. in Biomol NMR Assign 4:127–130, 2010. doi:10.1007/s12104-010-9227-8). That chimera, cTEM17m, held 17 amino acid substitutions relative to TEM-1 β-lactamase, resulting in a well-folded and fully functional protein with increased dynamics. Here we report the 1H, 13C and 15N 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. © 2015, Springer Science+Business Media Dordrecht.
| Type de document: | Article |
|---|---|
| Mots-clés libres: | Antibiotic resistance; Chimera; Protein engineering; PSE-4; TEM-1; β-Lactamase |
| Centre: | Centre INRS-Institut Armand Frappier |
| Date de dépôt: | 06 oct. 2017 13:59 |
| Dernière modification: | 21 févr. 2022 20:02 |
| URI: | https://espace.inrs.ca/id/eprint/4572 |
Gestion Actions (Identification requise)
 |
Modifier la notice |