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

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

doi:10.1038/s41467-021-22623-0

Nature Communications (May 2021)

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

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

Affiliations

Thierry Izoré: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University
Y. T. Candace Ho: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University
Joe A. Kaczmarski: Research School of Chemistry, The Australian National University
Athina Gavriilidou: Interfaculty Institute of Microbiology and Infection Medicine Tübingen, Microbiology/Biotechnology, University of Tübingen
Ka Ho Chow: School of Chemistry and Molecular Biosciences, The University of Queensland
David L. Steer: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University
Robert J. A. Goode: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University
Ralf B. Schittenhelm: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University
Julien Tailhades: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University
Manuela Tosin: Department of Chemistry, University of Warwick
Gregory L. Challis: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University
Elizabeth H. Krenske: School of Chemistry and Molecular Biosciences, The University of Queensland
Nadine Ziemert: German Centre for Infection Research (DZIF), Partnersite Tübingen
Colin J. Jackson: ARC Centre of Excellence for Innovations in Peptide and Protein Science
Max J. Cryle: Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University

DOI: https://doi.org/10.1038/s41467-021-22623-0
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 14

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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