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dc.contributor.authorLund, Bjarte Aarmo
dc.contributor.authorThomassen, Ane Molden
dc.contributor.authorCarlsen, Trine Josefine Olsen
dc.contributor.authorLeiros, Hanna-Kirsti S.
dc.date.accessioned2018-01-06T13:24:10Z
dc.date.available2018-01-06T13:24:10Z
dc.date.issued2017
dc.description.abstractThe first crystal structures of the class D β-lactamases OXA-181 and OXA-245 were determined to 2.05 and 2.20 Å resolution, respectively; in addition, the structure of a new crystal form of OXA-163 was resolved to 2.07 Å resolution. All of these enzymes are OXA-48-like and have been isolated from different clinical Klebsiella pneumoniae strains and also from other human pathogens such as Pseudomonas aeruginosa and Escherichia coli. Here, enzyme kinetics and thermostability studies are presented, and the new crystal structures are used to explain the observed variations. OXA-245 had the highest melting point (T<sub>m</sub> = 55.8°C), as determined by differential scanning calorimetry, compared with OXA-163 (T<sub>m</sub> = 49.4°C) and OXA-181 (T<sub>m</sub> = 52.6°C). The differences could be explained by the loss of two salt bridges in OXA-163, and an overall decrease in the polarity of the surface of OXA-181 compared with OXA-245.en_US
dc.descriptionSource at <a href=https://doi.org/10.1107/S2053230X17013838> https://doi.org/10.1107/S2053230X17013838 </a>en_US
dc.identifier.citationLund BA, Thomassen AM, Carlsen TJO, Leiros HKS. Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2017;73(10):579-587en_US
dc.identifier.cristinIDFRIDAID 1501601
dc.identifier.doi10.1107/s2053230x17013838
dc.identifier.issn1744-3091
dc.identifier.urihttps://hdl.handle.net/10037/11919
dc.language.isoengen_US
dc.publisherInternational Union of Crystallographyen_US
dc.relation.journalActa Crystallographica. Section F : Structural Biology and Crystallization Communications
dc.rights.accessRightsopenAccessen_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Fysikk: 430::Atomfysikk, molekylfysikk: 433en_US
dc.subjectVDP::Mathematics and natural science: 400::Physics: 430::Atomic physics, molecular physics: 433en_US
dc.titleStructure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysisen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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