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

DOI: 10.1002/1873-3468.13954 DOI Help

Authors: Waraporn Bunnak (Kasetsart University) , Ashley J. Winter (University of Bristol) , Colin M. Lazarus (University of Bristol) , Matthew P. Crump (University of Bristol) , Paul R. Race (University of Bristol) , Pakorn Wattana‐amorn (Kasetsart University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters

State: Published (Approved)
Published: October 2020
Diamond Proposal Number(s): 25819

Abstract: Menisporopsin A is a fungal bioactive macrocyclic polylactone, the biosynthesis of which requires only reducing (R) and non‐reducing (NR) polyketide synthases (PKSs) to guide a series of esterification and cyclolactonization reactions. There is 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‐a‐String 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.

Journal Keywords: macrocyclic polylactone; thioesterase; acyl carrier protein; fungal non‐reducing polyketide synthase; small angle X‐ray scattering

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: B21-High Throughput SAXS

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