SAXS reveals highly flexible interdomain linkers of tandem acyl carrier protein–thioesterase domains from a fungal non‐reducing polyketide synthase

Waraporn Bunnak, Ashley J Winter, Colin M Lazarus, Matthew P Crump, Paul R Race, Pakorn Wattana-Amorn

Research output: Contribution to journalArticle (Academic Journal)

Abstract

Menisporopsin A is a fungal bioactive macrocyclic polylactone requiring only reducing (R) and non-reducing (NR) polyketide synthases (PKSs) to guide a series of esterification and cyclolactonization reactions with no structural information pertaining to these PKSs. Here we report the solution characterization of singlet and doublet acyl carrier protein (ACP2 and ACP1-ACP2)-thioesterase (TE) domains from NR-PKS, involved in menisporopsin A biosynthesis. Small angle X-ray scattering (SAXS) studies in combination with homology modelling reveal that these polypeptides adopt a distinctive Beads-on-aString configuration, characterized by the presence of highly flexible interdomain linkers. These models provide a platform for studying domain organization and interdomain interactions in fungal NR-PKSs, which may be of value in directing the design of functionally optimised polyketide scaffolds.
Original languageEnglish
JournalFEBS Letters
Publication statusAccepted/In press - 5 Oct 2020

Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute

Keywords

  • macrocyclic polylactone
  • thioesterase
  • acyl carrier protein
  • fungal non-reducing polyketide synthase
  • small angle X-ray scattering

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