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


Journal Article

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 (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.

Full Text

Duke Authors

Cited Authors

  • Gobeil, SMC; Gagné, D; Doucet, N; Pelletier, JN

Published Date

  • April 2016

Published In

Volume / Issue

  • 10 / 1

Start / End Page

  • 93 - 99

PubMed ID

  • 26386961

Pubmed Central ID

  • 26386961

Electronic International Standard Serial Number (EISSN)

  • 1874-270X

International Standard Serial Number (ISSN)

  • 1874-2718

Digital Object Identifier (DOI)

  • 10.1007/s12104-015-9645-8


  • eng