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Cooperation between a T Domain and a Minimal C-Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS.

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Watzel J, Duchardt-Ferner E, Sarawi S, Bode HB, Wöhnert J
OpenAccess logo Angew Chem Int Ed Engl 60 14171-14178 (2021)
Cited: 2 times
EuropePMC logo PMID: 33876501

Abstract

Non-ribosomal peptide synthetases (NRPS) produce natural products from amino acid building blocks. They often consist of multiple polypeptide chains which assemble in a specific linear order via specialized N- and C-terminal docking domains (N/C DDs). Typically, docking domains function independently from other domains in NRPS assembly. Thus, docking domain replacements enable the assembly of "designer" NRPS from proteins that normally do not interact. The multiprotein "peptide-antimicrobial-Xenorhabdus" (PAX) peptide-producing PaxS NRPS is assembled from the three proteins PaxA, PaxB and PaxC. Herein, we show that the small C DD of PaxA cooperates with its preceding thiolation (T1 ) domain to bind the N DD of PaxB with very high affinity, establishing a structural and thermodynamical basis for this unprecedented docking interaction, and we test its functional importance in vivo in a truncated PaxS assembly line. Similar docking interactions are apparently present in other NRPS systems.

Articles - 7b2b mentioned but not cited (1)

  1. Cooperation between a T Domain and a Minimal C-Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS. Watzel J, Duchardt-Ferner E, Sarawi S, Bode HB, Wöhnert J. Angew Chem Int Ed Engl 60 14171-14178 (2021)


Articles citing this publication (1)

  1. Deletion of COM donor and acceptor domains and the interaction between modules in bacillomycin D produced by Bacillus amyloliquefaciens. Lv Z, Ma W, Zhang P, Lu Z, Zhou L, Meng F, Wang Z, Bie X. Synth Syst Biotechnol 7 989-1001 (2022)


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