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Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity
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Izoré, Thierry, Candace Ho, Y T, Kaczmarski, Joe A, Gavriilidou, Athina, Chow, Ka Ho, Steer, David L, Goode, Robert J A, Schittenhelm, Ralf B, Tailhades, Julien, Tosin, Manuela, Challis, Gregory L., Krenske, Elizabeth H, Ziemert, Nadine, Jackson, Colin J and Cryle, Max J (2021) Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity. Nature Communications, 12 (1). 2511. doi:10.1038/s41467-021-22623-0 ISSN 2041-1723.
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Official URL: https://doi.org/10.1038/s41467-021-22623-0
Abstract
Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots of a condensation domain in complex with an aminoacyl-PCP acceptor substrate. These structures allow the identification of a mechanism that controls access of acceptor substrates to the active site in condensation domains. The structures of this complex also allow us to demonstrate that condensation domain active sites do not contain a distinct pocket to select the side chain of the acceptor substrate during peptide assembly but that residues within the active site motif can instead serve to tune the selectivity of these central biosynthetic domains.
| Item Type: | Journal Article | ||||||
|---|---|---|---|---|---|---|---|
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||
| SWORD Depositor: | Library Publications Router | ||||||
| Journal or Publication Title: | Nature Communications | ||||||
| Publisher: | Nature Publishing Group | ||||||
| ISSN: | 2041-1723 | ||||||
| Official Date: | 4 May 2021 | ||||||
| Dates: |
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| Volume: | 12 | ||||||
| Number: | 1 | ||||||
| Article Number: | 2511 | ||||||
| DOI: | 10.1038/s41467-021-22623-0 | ||||||
| Status: | Peer Reviewed | ||||||
| Publication Status: | Published | ||||||
| Access rights to Published version: | Open Access (Creative Commons) | ||||||
| Is Part Of: | 1 |
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