Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam.

ABSTRACT: Backbone chemical shift assignments for the Toho-1 β-lactamase (263 amino acids, 28.9 kDa) are reported based on triple resonance solution-state NMR experiments performed on a uniformly ²H,¹³C,¹⁵N-labeled sample. These assignments allow for subsequent site-specific characterization at the chemical, structural, and dynamical levels. At the chemical level, titration with the non-β-lactam β-lactamase inhibitor avibactam is found to give chemical shift perturbations indicative of tight covalent binding that allow for mapping of the inhibitor binding site. At the structural level, protein secondary structure is predicted based on the backbone chemical shifts and protein residue sequence using TALOS-N and found to agree well with structural characterization from

SUBMITTER: Sakhrani VV 

PROVIDER: S-EPMC9122098 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature