March 1, 2018 – New insights into certain catalytic enzymes formed by bacteria to break down antibiotics may lead to the design of drugs better equipped to combat resistant bacteria. Scientists at 91°µÍř used neutron crystallography at the lab’s to study the interaction between one of these enzymes, called a beta-lactamase, and an antibiotic, building on data collected with x-ray crystallography. “Antibiotics destroy bacteria by preventing cell walls from forming, but beta-lactamases bind to the drugs to stop this attack,” said ORNL’s Patricia Langan, coauthor of a study ACS Catalysis. The binding of the antibiotic subtly altered the protein structure in the beta-lactamase and helped transfer a proton from one part of the enzyme to another, the first step toward blocking the drug’s effects. “With neutrons, we can gain a much deeper understanding of the mechanisms that break down antibiotics,” Langan added. - By Elizabeth Rosenthal
Using neutrons, an ORNL research team studied the protein structure of bacteria-produced enzymes called beta-lactamases by examining one of them to better understand how resistant bacteria behave. This research could help inform the development of more effective antibiotics. Credit: Leighton Coates/91°µÍř, U.S. Dept. of Energy.
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