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

Lookup NU author(s): Professor Paul RaceORCiD

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Abstract

© 2020 Federation of European Biochemical Societies. Menisporopsin A is a fungal bioactive macrocyclic polylactone, the biosynthesis of which requires only reducing (R) and nonreducing (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 optimized polyketide scaffolds.

Publication metadata

Author(s): Bunnak W, Winter AJ, Lazarus CM, Crump MP, Race PR, Wattana-Amorn P

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2021

Volume: 595

Issue: 1

Pages: 133-144

Print publication date: 01/01/2021

Online publication date: 12/10/2020

Acceptance date: 05/10/2020

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: Wiley-Blackwell

URL: https://doi.org/10.1002/1873-3468.13954

DOI: 10.1002/1873-3468.13954

PubMed id: 33043457

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