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

ABSTRACT: The widespread use of ?-lactam antibiotics has given rise to a dramatic increase in clinically-relevant ?-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 ?-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 ?-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.

SUBMITTER: Gobeil SM 

PROVIDER: S-EPMC5419827 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature