AI Article Synopsis
- The rise of β-lactam antibiotics has led to a significant increase in β-lactamases, making it crucial to understand their structure and function to combat antibiotic resistance.
- Researchers previously characterized a chimeric β-lactamase, cTEM17m, which had 17 amino acid substitutions from TEM-1, resulting in a functional protein with enhanced dynamics.
- This study presents the backbone resonance assignments of another chimera, cTEM-19m, featuring 19 substitutions and notable active-site changes, aiming to analyze their dynamic behaviors.
Article Abstract
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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5419827 | PMC |
| http://dx.doi.org/10.1007/s12104-015-9645-8 | DOI Listing |
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