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

Autor: Ketan D. Patel, Felipe B. d’Andrea, Nicole M. Gaudelli, Andrew R. Buller, Craig A. Townsend, Andrew M. Gulick
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/s41467-019-11740-6
Popis: 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.
Databáze: Directory of Open Access Journals