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  • Hakulinen, Jonna K (author)

MraY-antibiotic complex reveals details of tunicamycin mode of action.

  • Article/chapterEnglish2017

Publisher, publication year, extent ...

  • 2017-01-09
  • Springer Science and Business Media LLC,2017

Numbers

  • LIBRIS-ID:oai:gup.ub.gu.se/249615
  • https://gup.ub.gu.se/publication/249615URI
  • https://doi.org/10.1038/nchembio.2270DOI

Supplementary language notes

  • Language:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Hering, JennyGothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xherje (author)
  • Brändén, Gisela,1975Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xbragi (author)
  • Chen, Hongming (author)
  • Snijder, Arjan (author)
  • Ek, Margareta (author)
  • Johansson, Patrik (author)
  • Göteborgs universitetInstitutionen för kemi och molekylärbiologi (creator_code:org_t)

Related titles

  • In:Nature chemical biology: Springer Science and Business Media LLC13:3, s. 265-2671552-44691552-4450

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