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

Ben C. Chung, Ellene H. Mashalidis, Tetsuya Tanino, Mijung Kim, Akira Matsuda, Jiyong Hong, Satoshi Ichikawa and Seok-Yong Lee ()
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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

Nature, 2016, vol. 533, issue 7604, 557-560

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.

Date: 2016
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DOI: 10.1038/nature17636

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