Probing the role of the conserved residue Glu166 in a class A β-lactamase using neutron and X-ray protein crystallography.

ABSTRACT: The amino-acid sequence of the Toho-1 β-lactamase contains several conserved residues in the active site, including Ser70, Lys73, Ser130 and Glu166, some of which coordinate a catalytic water molecule. This catalytic water molecule is essential in the acylation and deacylation parts of the reaction mechanism through which Toho-1 inactivates specific antibiotics and provides resistance to its expressing bacterial strains. To investigate the function of Glu166 in the acylation part of the catalytic mechanism, neutron and X-ray crystallographic studies were performed on a Glu166Gln mutant. The structure of this class A β-lactamase mutant provides several insights into its previously reported reduced drug-binding kinetic rates. A joint refinement of both X-ray and neutron diffraction data was

SUBMITTER: Langan PS 

PROVIDER: S-EPMC7008513 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature