7ODA

OXA-48-like Beta-lactamase OXA-436

Summary for 7ODA

• Entry DOI: 10.2210/pdb7oda/pdb
• Descriptor: Beta-lactamase, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: beta-lactamase, hydrolase, antibiotic resistance
• Biological source: Enterobacter asburiae
• Total number of polymer chains: 4
• Total formula weight: 113269.05

Authors

Lund, B.A.,Thomassen, A.M.,Carlsen, T.J.W.,Leiros, H.K.S. (deposition date: 2021-04-29, release date: 2021-09-08, Last modification date: 2024-01-31)

Primary citation

Lund, B.A.,Thomassen, A.M.,Carlsen, T.J.W.,Leiros, H.K.S.
Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436.
Acta Crystallogr.,Sect.F, 77:312-318, 2021

PubMed Abstract: The crystal structure of the class D β-lactamase OXA-436 was solved to a resolution of 1.80 Å. 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 α3-α4 and β5-β6 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.

PubMed: 34473108
DOI: 10.1107/S2053230X21008645

Experimental method

X-RAY DIFFRACTION (1.796 Å)