Published in January 2017 by Dr Margareta Ek Group (Structural, dynamical and inhibitor studies of membrane proteins)

MraY–antibiotic complex reveals details of tunicamycin mode of action
Hakulinen J.K., Hering J., Brändén G., Chen H., Snijder A., Ek M., Johansson K
Published online– PMID: 28068312 DOI: 10.1038/nchembio.2270

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.