1H, 13C, and 15N backbone resonance assignments for KPC-2, a class A serine-β-lactamase.
The ever-increasing occurrence of antibiotic resistance presents a major threat to public health. Specifically, resistance conferred by β-lactamases places the efficacy of currently available antibiotics at risk. Klebsiella pneumoniae carbapenemase-2 (KPC-2) is a β-lactamase that enables carbapenem resistance and represents a clear and present danger to global public health. In order to combat bacterial infections harboring KPC-2 expression, inhibitors with improved potency need to be developed. Although the structure of KPC-2 has been solved by X-ray crystallography, NMR provides the unique opportunity to study the structure and dynamics of flexible loop regions in solution. Here we report the 1H, 13C, and 15N backbone chemical shift assignments for KPC-2 in the apo state as the first step towards the study of KPC-2 dynamics in the presence and absence of ligands to enable the rational design of optimized inhibitors.
['VanPelt|Jamie|J|', 'Shurina|Ben A|BA|', 'Ramelot|Theresa A|TA|', 'Bonomo|Robert A|RA|', 'Page|Richard C|RC|http://orcid.org/0000-0002-3006-3171']
D002247:Carbon Isotopes D009587:Nitrogen Isotopes D019906:Nuclear Magnetic Resonance, Biomolecular D017433:Protein Structure, Secondary D011522:Protons D001618:beta-Lactamases
KPC-2 Antibiotic resistance β-Lactamase NMR Carbapenamase