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Structural insights into inhibition of lipid I production in bacterial cell wall synthesis

Author

Listed:
  • Ben C. Chung

    (Duke University Medical Center)

  • Ellene H. Mashalidis

    (Duke University Medical Center)

  • Tetsuya Tanino

    (Faculty of Pharmaceutical Sciences, Hokkaido University)

  • Mijung Kim

    (Duke University)

  • Akira Matsuda

    (Faculty of Pharmaceutical Sciences, Hokkaido University)

  • Jiyong Hong

    (Duke University)

  • Satoshi Ichikawa

    (Faculty of Pharmaceutical Sciences, Hokkaido University)

  • Seok-Yong Lee

    (Duke University Medical Center)

Abstract

The crystal structure of the MraY enzyme from Aquifex aeolicus in complex with the naturally occurring nucleoside inhibitor muraymycin D2 (MD2) reveals that MraY undergoes a large conformational rearrangement near the active site after the binding of MD2, leading to the generation of a nucleoside-binding pocket and a peptide-binding site.

Suggested Citation

  • Ben C. Chung & Ellene H. Mashalidis & Tetsuya Tanino & Mijung Kim & Akira Matsuda & Jiyong Hong & Satoshi Ichikawa & Seok-Yong Lee, 2016. "Structural insights into inhibition of lipid I production in bacterial cell wall synthesis," Nature, Nature, vol. 533(7604), pages 557-560, May.
    • Handle: RePEc:nat:nature:v:533:y:2016:i:7604:d:10.1038_nature17636
    DOI: 10.1038/nature17636
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    Cited by:

    1. Abraham O. Oluwole & Robin A. Corey & Chelsea M. Brown & Victor M. Hernández-Rocamora & Phillip J. Stansfeld & Waldemar Vollmer & Jani R. Bolla & Carol V. Robinson, 2022. "Peptidoglycan biosynthesis is driven by lipid transfer along enzyme-substrate affinity gradients," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Takeshi Nakaya & Miyuki Yabe & Ellene H. Mashalidis & Toyotaka Sato & Kazuki Yamamoto & Yuta Hikiji & Akira Katsuyama & Motoko Shinohara & Yusuke Minato & Satoshi Takahashi & Motohiro Horiuchi & Shin-, 2022. "Synthesis of macrocyclic nucleoside antibacterials and their interactions with MraY," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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