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The biological assembly of OXA-48 reveals a dimer interface with high charge complementarity and very high affinity.
Lund, Bjarte Aarmo; Thomassen, Ane Molden; Nesheim, Birgit Helene Berg; Carlsen, Trine Josefine Olsen; Isaksson, Johan; Christopeit, Tony; Leiros, Hanna-Kirsti S.
Affiliation
  • Lund BA; Department of Chemistry, Faculty of Science and Technology, The Norwegian Structural Biology Centre (NorStruct), UiT The Arctic University of Norway, Tromsø, Norway.
  • Thomassen AM; Department of Chemistry, Faculty of Science and Technology, The Norwegian Structural Biology Centre (NorStruct), UiT The Arctic University of Norway, Tromsø, Norway.
  • Nesheim BHB; Department of Chemistry, Faculty of Science and Technology, The Norwegian Structural Biology Centre (NorStruct), UiT The Arctic University of Norway, Tromsø, Norway.
  • Carlsen TJO; Department of Chemistry, Faculty of Science and Technology, The Norwegian Structural Biology Centre (NorStruct), UiT The Arctic University of Norway, Tromsø, Norway.
  • Isaksson J; Department of Chemistry, Faculty of Science and Technology, UiT The Arctic University of Norway, Tromsø, Norway.
  • Christopeit T; Department of Chemistry, Faculty of Science and Technology, The Norwegian Structural Biology Centre (NorStruct), UiT The Arctic University of Norway, Tromsø, Norway.
  • Leiros HS; Department of Chemistry, Faculty of Science and Technology, The Norwegian Structural Biology Centre (NorStruct), UiT The Arctic University of Norway, Tromsø, Norway.
FEBS J ; 285(22): 4214-4228, 2018 11.
Article in En | MEDLINE | ID: mdl-30153368
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Beta-Lactamases / Escherichia coli Proteins / Protein Multimerization / Mutation Language: En Journal: FEBS J Journal subject: BIOQUIMICA Year: 2018 Document type: Article Affiliation country: Country of publication:
Fulltext
Add to My VHL
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Beta-Lactamases / Escherichia coli Proteins / Protein Multimerization / Mutation Language: En Journal: FEBS J Journal subject: BIOQUIMICA Year: 2018 Document type: Article Affiliation country: Country of publication: