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Publication Abstract from PubMed

The crystal structure of the class D beta-lactamase OXA-436 was solved to a resolution of 1.80 A. Higher catalytic rates were found at higher temperatures for the clinically important antibiotic imipenem, indicating better adaptation of OXA-436 to its mesophilic host than OXA-48, which is believed to originate from an environmental source. Furthermore, based on the most populated conformations during 100 ns molecular-dynamics simulations, it is postulated that the modulation of activity involves conformational shifts of the alpha3-alpha4 and beta5-beta6 loops. While these changes overall do not cause clinically significant shifts in the resistance profile, they show that antibiotic-resistance enzymes exist in a continuum. It is believed that these seemingly neutral differences in the sequence exist on a path leading to significant changes in substrate selectivity.

Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436.,Lund BA, Thomassen AM, Carlsen TJW, Leiros HKS Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):312-318. doi:, 10.1107/S2053230X21008645. Epub 2021 Aug 31. PMID:34473108^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.