Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS

Rhabdopeptides are synthesized by non-ribosomal peptide synthetases (NRPSs) and the multiple NRPS subunits interact through docking domains (DD). Here the authors provide insights into DD interaction patterns and present the structures of three N-terminal docking domains (NDD) and a NDD-CDD complex...

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Autores principales:	Carolin Hacker, Xiaofeng Cai, Carsten Kegler, Lei Zhao, A. Katharina Weickhmann, Jan Philip Wurm, Helge B. Bode, Jens Wöhnert
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/50bf087ff2d641078edc19018ffe02fd
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spelling	oai:doaj.org-article:50bf087ff2d641078edc19018ffe02fd2021-12-02T15:34:01ZStructure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS10.1038/s41467-018-06712-12041-1723https://doaj.org/article/50bf087ff2d641078edc19018ffe02fd2018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06712-1https://doaj.org/toc/2041-1723Rhabdopeptides are synthesized by non-ribosomal peptide synthetases (NRPSs) and the multiple NRPS subunits interact through docking domains (DD). Here the authors provide insights into DD interaction patterns and present the structures of three N-terminal docking domains (NDD) and a NDD-CDD complex and derive a set of recognition rules for DD interactions.Carolin HackerXiaofeng CaiCarsten KeglerLei ZhaoA. Katharina WeickhmannJan Philip WurmHelge B. BodeJens WöhnertNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Carolin Hacker Xiaofeng Cai Carsten Kegler Lei Zhao A. Katharina Weickhmann Jan Philip Wurm Helge B. Bode Jens Wöhnert Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS
description	Rhabdopeptides are synthesized by non-ribosomal peptide synthetases (NRPSs) and the multiple NRPS subunits interact through docking domains (DD). Here the authors provide insights into DD interaction patterns and present the structures of three N-terminal docking domains (NDD) and a NDD-CDD complex and derive a set of recognition rules for DD interactions.
format	article
author	Carolin Hacker Xiaofeng Cai Carsten Kegler Lei Zhao A. Katharina Weickhmann Jan Philip Wurm Helge B. Bode Jens Wöhnert
author_facet	Carolin Hacker Xiaofeng Cai Carsten Kegler Lei Zhao A. Katharina Weickhmann Jan Philip Wurm Helge B. Bode Jens Wöhnert
author_sort	Carolin Hacker
title	Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS
title_short	Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS
title_full	Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS
title_fullStr	Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS
title_full_unstemmed	Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS
title_sort	structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing nrps
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/50bf087ff2d641078edc19018ffe02fd
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Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS

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