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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2021
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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) |
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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 |
work_keys_str_mv |
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