Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions

NocTE is a nonribosomal peptide synthetase thioesterase that completes the biosynthesis of pro-nocardicin G, the precursor for nocardicin β-lactam antibiotics. Here the authors provide mechanistic insights into NocTE by determining its crystal structures in the ligand-free form and covalently linked...

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Autores principales:	Ketan D. Patel, Felipe B. d’Andrea, Nicole M. Gaudelli, Andrew R. Buller, Craig A. Townsend, Andrew M. Gulick
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0edee8fbfb374cbf8bab9f96d03b7963
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spelling	oai:doaj.org-article:0edee8fbfb374cbf8bab9f96d03b79632021-12-02T14:39:03ZStructure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions10.1038/s41467-019-11740-62041-1723https://doaj.org/article/0edee8fbfb374cbf8bab9f96d03b79632019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11740-6https://doaj.org/toc/2041-1723NocTE is a nonribosomal peptide synthetase thioesterase that completes the biosynthesis of pro-nocardicin G, the precursor for nocardicin β-lactam antibiotics. Here the authors provide mechanistic insights into NocTE by determining its crystal structures in the ligand-free form and covalently linked to a fluorophosphonate substrate mimic.Ketan D. PatelFelipe B. d’AndreaNicole M. GaudelliAndrew R. BullerCraig A. TownsendAndrew M. GulickNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ketan D. Patel Felipe B. d’Andrea Nicole M. Gaudelli Andrew R. Buller Craig A. Townsend Andrew M. Gulick Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions
description	NocTE is a nonribosomal peptide synthetase thioesterase that completes the biosynthesis of pro-nocardicin G, the precursor for nocardicin β-lactam antibiotics. Here the authors provide mechanistic insights into NocTE by determining its crystal structures in the ligand-free form and covalently linked to a fluorophosphonate substrate mimic.
format	article
author	Ketan D. Patel Felipe B. d’Andrea Nicole M. Gaudelli Andrew R. Buller Craig A. Townsend Andrew M. Gulick
author_facet	Ketan D. Patel Felipe B. d’Andrea Nicole M. Gaudelli Andrew R. Buller Craig A. Townsend Andrew M. Gulick
author_sort	Ketan D. Patel
title	Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions
title_short	Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions
title_full	Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions
title_fullStr	Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions
title_full_unstemmed	Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions
title_sort	structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/0edee8fbfb374cbf8bab9f96d03b7963
work_keys_str_mv	AT ketandpatel structureofaboundpeptidephosphonaterevealsthemechanismofnocardicinbifunctionalthioesteraseepimerasehydrolasehalfreactions AT felipebdandrea structureofaboundpeptidephosphonaterevealsthemechanismofnocardicinbifunctionalthioesteraseepimerasehydrolasehalfreactions AT nicolemgaudelli structureofaboundpeptidephosphonaterevealsthemechanismofnocardicinbifunctionalthioesteraseepimerasehydrolasehalfreactions AT andrewrbuller structureofaboundpeptidephosphonaterevealsthemechanismofnocardicinbifunctionalthioesteraseepimerasehydrolasehalfreactions AT craigatownsend structureofaboundpeptidephosphonaterevealsthemechanismofnocardicinbifunctionalthioesteraseepimerasehydrolasehalfreactions AT andrewmgulick structureofaboundpeptidephosphonaterevealsthemechanismofnocardicinbifunctionalthioesteraseepimerasehydrolasehalfreactions
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Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions

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