Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics
Kistamicin is a structurally divergent glycopeptide antibiotic (GPA) that contains a unique 15-membered A-O-B ring. Here, the authors obtained a crystal structure of the kistamicin OxyA/X-domain complex and analysed the cyclisation cascade leading to the formation of the A-O-B ring.
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Nature Portfolio
2019
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oai:doaj.org-article:09b465696c784ff3b63bbdc04e4fd0ff2021-12-02T14:40:18ZKistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics10.1038/s41467-019-10384-w2041-1723https://doaj.org/article/09b465696c784ff3b63bbdc04e4fd0ff2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10384-whttps://doaj.org/toc/2041-1723Kistamicin is a structurally divergent glycopeptide antibiotic (GPA) that contains a unique 15-membered A-O-B ring. Here, the authors obtained a crystal structure of the kistamicin OxyA/X-domain complex and analysed the cyclisation cascade leading to the formation of the A-O-B ring.Anja GreuleThierry IzoréDumitrita IftimeJulien TailhadesMelanie SchoppetYongwei ZhaoMadeleine PeschkeIftekhar AhmedAndreas KulikMartina AdamekRobert J. A. GoodeRalf B. SchittenhelmJoe A. KaczmarskiColin J. JacksonNadine ZiemertElizabeth H. KrenskeJames J. De VossEvi StegmannMax J. CryleNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019) |
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Science Q Anja Greule Thierry Izoré Dumitrita Iftime Julien Tailhades Melanie Schoppet Yongwei Zhao Madeleine Peschke Iftekhar Ahmed Andreas Kulik Martina Adamek Robert J. A. Goode Ralf B. Schittenhelm Joe A. Kaczmarski Colin J. Jackson Nadine Ziemert Elizabeth H. Krenske James J. De Voss Evi Stegmann Max J. Cryle Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics |
description |
Kistamicin is a structurally divergent glycopeptide antibiotic (GPA) that contains a unique 15-membered A-O-B ring. Here, the authors obtained a crystal structure of the kistamicin OxyA/X-domain complex and analysed the cyclisation cascade leading to the formation of the A-O-B ring. |
format |
article |
author |
Anja Greule Thierry Izoré Dumitrita Iftime Julien Tailhades Melanie Schoppet Yongwei Zhao Madeleine Peschke Iftekhar Ahmed Andreas Kulik Martina Adamek Robert J. A. Goode Ralf B. Schittenhelm Joe A. Kaczmarski Colin J. Jackson Nadine Ziemert Elizabeth H. Krenske James J. De Voss Evi Stegmann Max J. Cryle |
author_facet |
Anja Greule Thierry Izoré Dumitrita Iftime Julien Tailhades Melanie Schoppet Yongwei Zhao Madeleine Peschke Iftekhar Ahmed Andreas Kulik Martina Adamek Robert J. A. Goode Ralf B. Schittenhelm Joe A. Kaczmarski Colin J. Jackson Nadine Ziemert Elizabeth H. Krenske James J. De Voss Evi Stegmann Max J. Cryle |
author_sort |
Anja Greule |
title |
Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics |
title_short |
Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics |
title_full |
Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics |
title_fullStr |
Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics |
title_full_unstemmed |
Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics |
title_sort |
kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics |
publisher |
Nature Portfolio |
publishDate |
2019 |
url |
https://doaj.org/article/09b465696c784ff3b63bbdc04e4fd0ff |
work_keys_str_mv |
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