Show simple item record

dc.contributor.authorLund, Bjarte Aarmo
dc.contributor.authorThomassen, Ane Molden
dc.contributor.authorCarlsen, Trine Josefine Warg
dc.contributor.authorLeiros, Hanna-Kirsti Schrøder
dc.date.accessioned2021-09-08T06:30:58Z
dc.date.available2021-09-08T06:30:58Z
dc.date.issued2021-08-31
dc.description.abstractThe 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.en_US
dc.identifier.citationLund, Thomassen, Carlsen, Leiros. Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2021en_US
dc.identifier.cristinIDFRIDAID 1930658
dc.identifier.doi10.1107/S2053230X21008645
dc.identifier.issn1744-3091
dc.identifier.urihttps://hdl.handle.net/10037/22440
dc.language.isoengen_US
dc.publisherInternational Union of Crystallographyen_US
dc.relation.journalActa Crystallographica. Section F : Structural Biology and Crystallization Communications
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/SFF/262695/Norway/Hylleraas Centre for Quantum Molecular Sciences//en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/FRINATEK/274858/Norway/Evolutionary Principles of Biocatalysts From Extreme Environments//en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/BEDREHELSE/273332/Norway/Inhibition of clinically relevant carbapenemases/ICARBA/en_US
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2021 The Author(s)en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440en_US
dc.titleBiochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436en_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


File(s) in this item

Thumbnail

This item appears in the following collection(s)

Show simple item record