Chemical logic of MraY inhibition by antibacterial nucleoside natural products

Phospho-MurNAc-pentapeptide translocase (MraY) is a bacterial integral membrane enzyme that is essential for peptidoglycan biosynthesis. Here the authors present the crystal structures of MraY from Aquifex aeolicus bound to caprazamycin, capuramycin and mureidomycin and discuss the implications for...

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Autores principales: Ellene H. Mashalidis, Benjamin Kaeser, Yuma Terasawa, Akira Katsuyama, Do-Yeon Kwon, Kiyoun Lee, Jiyong Hong, Satoshi Ichikawa, Seok-Yong Lee
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/e0558f6d0eab41fcbb345629cf908792
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spelling oai:doaj.org-article:e0558f6d0eab41fcbb345629cf9087922021-12-02T15:35:53ZChemical logic of MraY inhibition by antibacterial nucleoside natural products10.1038/s41467-019-10957-92041-1723https://doaj.org/article/e0558f6d0eab41fcbb345629cf9087922019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10957-9https://doaj.org/toc/2041-1723Phospho-MurNAc-pentapeptide translocase (MraY) is a bacterial integral membrane enzyme that is essential for peptidoglycan biosynthesis. Here the authors present the crystal structures of MraY from Aquifex aeolicus bound to caprazamycin, capuramycin and mureidomycin and discuss the implications for antibiotic development.Ellene H. MashalidisBenjamin KaeserYuma TerasawaAkira KatsuyamaDo-Yeon KwonKiyoun LeeJiyong HongSatoshi IchikawaSeok-Yong LeeNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Ellene H. Mashalidis
Benjamin Kaeser
Yuma Terasawa
Akira Katsuyama
Do-Yeon Kwon
Kiyoun Lee
Jiyong Hong
Satoshi Ichikawa
Seok-Yong Lee
Chemical logic of MraY inhibition by antibacterial nucleoside natural products
description Phospho-MurNAc-pentapeptide translocase (MraY) is a bacterial integral membrane enzyme that is essential for peptidoglycan biosynthesis. Here the authors present the crystal structures of MraY from Aquifex aeolicus bound to caprazamycin, capuramycin and mureidomycin and discuss the implications for antibiotic development.
format article
author Ellene H. Mashalidis
Benjamin Kaeser
Yuma Terasawa
Akira Katsuyama
Do-Yeon Kwon
Kiyoun Lee
Jiyong Hong
Satoshi Ichikawa
Seok-Yong Lee
author_facet Ellene H. Mashalidis
Benjamin Kaeser
Yuma Terasawa
Akira Katsuyama
Do-Yeon Kwon
Kiyoun Lee
Jiyong Hong
Satoshi Ichikawa
Seok-Yong Lee
author_sort Ellene H. Mashalidis
title Chemical logic of MraY inhibition by antibacterial nucleoside natural products
title_short Chemical logic of MraY inhibition by antibacterial nucleoside natural products
title_full Chemical logic of MraY inhibition by antibacterial nucleoside natural products
title_fullStr Chemical logic of MraY inhibition by antibacterial nucleoside natural products
title_full_unstemmed Chemical logic of MraY inhibition by antibacterial nucleoside natural products
title_sort chemical logic of mray inhibition by antibacterial nucleoside natural products
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/e0558f6d0eab41fcbb345629cf908792
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AT kiyounlee chemicallogicofmrayinhibitionbyantibacterialnucleosidenaturalproducts
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AT satoshiichikawa chemicallogicofmrayinhibitionbyantibacterialnucleosidenaturalproducts
AT seokyonglee chemicallogicofmrayinhibitionbyantibacterialnucleosidenaturalproducts
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