Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity

Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes assembling complex natural products. Here, the structures of a Thermobifida fusca NRPS condensation domain bound to the substrate-bearing peptidyl carrier protein (PCP) domain provide insight into the mechanisms of substrate selecti...

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Autores principales: Thierry Izoré, Y. T. Candace Ho, Joe A. Kaczmarski, Athina Gavriilidou, Ka Ho Chow, David L. Steer, Robert J. A. Goode, Ralf B. Schittenhelm, Julien Tailhades, Manuela Tosin, Gregory L. Challis, Elizabeth H. Krenske, Nadine Ziemert, Colin J. Jackson, Max J. Cryle
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/fbb66a8fa3204b6a841066cc1c1e62db
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spelling oai:doaj.org-article:fbb66a8fa3204b6a841066cc1c1e62db2021-12-02T16:51:30ZStructures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity10.1038/s41467-021-22623-02041-1723https://doaj.org/article/fbb66a8fa3204b6a841066cc1c1e62db2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22623-0https://doaj.org/toc/2041-1723Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes assembling complex natural products. Here, the structures of a Thermobifida fusca NRPS condensation domain bound to the substrate-bearing peptidyl carrier protein (PCP) domain provide insight into the mechanisms of substrate selectivity and engagement within the catalytic pocket.Thierry IzoréY. T. Candace HoJoe A. KaczmarskiAthina GavriilidouKa Ho ChowDavid L. SteerRobert J. A. GoodeRalf B. SchittenhelmJulien TailhadesManuela TosinGregory L. ChallisElizabeth H. KrenskeNadine ZiemertColin J. JacksonMax J. CryleNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Thierry Izoré
Y. T. Candace Ho
Joe A. Kaczmarski
Athina Gavriilidou
Ka Ho Chow
David L. Steer
Robert J. A. Goode
Ralf B. Schittenhelm
Julien Tailhades
Manuela Tosin
Gregory L. Challis
Elizabeth H. Krenske
Nadine Ziemert
Colin J. Jackson
Max J. Cryle
Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
description Non-ribosomal peptide synthetases (NRPSs) are multi-modular enzymes assembling complex natural products. Here, the structures of a Thermobifida fusca NRPS condensation domain bound to the substrate-bearing peptidyl carrier protein (PCP) domain provide insight into the mechanisms of substrate selectivity and engagement within the catalytic pocket.
format article
author Thierry Izoré
Y. T. Candace Ho
Joe A. Kaczmarski
Athina Gavriilidou
Ka Ho Chow
David L. Steer
Robert J. A. Goode
Ralf B. Schittenhelm
Julien Tailhades
Manuela Tosin
Gregory L. Challis
Elizabeth H. Krenske
Nadine Ziemert
Colin J. Jackson
Max J. Cryle
author_facet Thierry Izoré
Y. T. Candace Ho
Joe A. Kaczmarski
Athina Gavriilidou
Ka Ho Chow
David L. Steer
Robert J. A. Goode
Ralf B. Schittenhelm
Julien Tailhades
Manuela Tosin
Gregory L. Challis
Elizabeth H. Krenske
Nadine Ziemert
Colin J. Jackson
Max J. Cryle
author_sort Thierry Izoré
title Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
title_short Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
title_full Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
title_fullStr Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
title_full_unstemmed Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
title_sort structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/fbb66a8fa3204b6a841066cc1c1e62db
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