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MraY-antibiotic complex reveals details of tunicamycin mode of action.
Hakulinen, Jonna K; Hering, Jenny; Brändén, Gisela; Chen, Hongming; Snijder, Arjan; Ek, Margareta; Johansson, Patrik.
Afiliação
  • Hakulinen JK; Discovery Sciences, Innovative Medicines and Early Development Biotech Unit, AstraZeneca R&D Gothenburg, Gothenburg, Sweden.
  • Hering J; Discovery Sciences, Innovative Medicines and Early Development Biotech Unit, AstraZeneca R&D Gothenburg, Gothenburg, Sweden.
  • Brändén G; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Chen H; Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Snijder A; Discovery Sciences, Innovative Medicines and Early Development Biotech Unit, AstraZeneca R&D Gothenburg, Gothenburg, Sweden.
  • Ek M; Discovery Sciences, Innovative Medicines and Early Development Biotech Unit, AstraZeneca R&D Gothenburg, Gothenburg, Sweden.
  • Johansson P; Discovery Sciences, Innovative Medicines and Early Development Biotech Unit, AstraZeneca R&D Gothenburg, Gothenburg, Sweden.
Nat Chem Biol ; 13(3): 265-267, 2017 03.
Article em En | MEDLINE | ID: mdl-28068312
ABSTRACT
The rapid increase of antibiotic resistance has created an urgent need to develop novel antimicrobial agents. Here we describe the crystal structure of the promising bacterial target phospho-N-acetylmuramoyl-pentapeptide translocase (MraY) in complex with the nucleoside antibiotic tunicamycin. The structure not only reveals the mode of action of several related natural-product antibiotics but also gives an indication on the binding mode of the MraY UDP-MurNAc-pentapeptide and undecaprenyl-phosphate substrates.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2017 Tipo de documento: Article