Kistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics

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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Detalles Bibliográficos
Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Science
Q
Acceso en línea:https://doaj.org/article/09b465696c784ff3b63bbdc04e4fd0ff
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Sumario: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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