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

Journal article
Authors Jonna K Hakulinen
Jenny Hering
Gisela Brändén
Hongming Chen
Arjan Snijder
Margareta Ek
Patrik Johansson
Published in Nature chemical biology
Volume 13
Pages 265–267
ISSN 1552-4469
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Pages 265–267
Language en
Links dx.doi.org/10.1038/nchembio.2270
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Structural Biology, Biochemistry, Microbiology

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.

Page Manager: Webmaster|Last update: 9/11/2012
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