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15N, 13C and 1H backbone resonance assignments of an artificially engineered TEM-1/PSE-4 class A β-lactamase chimera and its deconvoluted mutant

Gobeil, Sophie M.C.; Gagné, Donald; Doucet, Nicolas; 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. p. 93-99. DOI: 10.1007/s12104-015-9645-8.

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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: 06 oct. 2017 13:59
URI: http://espace.inrs.ca/id/eprint/4572

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