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There is no structural information pertaining to these PKSs. Here, we report the solution characterization of singlet and doublet acyl carrier protein (ACP<jats:sub>2<\/jats:sub> and ACP<jats:sub>1<\/jats:sub>\u2010ACP<jats:sub>2<\/jats:sub>)\u2013thioesterase (TE) domains from NR\u2010PKS involved in menisporopsin A biosynthesis. Small\u2010angle X\u2010ray scattering (SAXS) studies in combination with homology modelling reveal that these polypeptides adopt a distinctive beads\u2010on\u2010a\u2010string 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\u2010PKSs, which may be of value in directing the design of functionally optimized polyketide scaffolds.<\/jats:p>","DOI":"10.1002\/1873-3468.13954","type":"journal-article","created":{"date-parts":[[2020,10,12]],"date-time":"2020-10-12T08:46:22Z","timestamp":1602492382000},"page":"133-144","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["SAXS reveals highly flexible interdomain linkers of tandem acyl carrier protein\u2013thioesterase domains from a fungal nonreducing polyketide synthase"],"prefix":"10.1002","volume":"595","author":[{"given":"Waraporn","family":"Bunnak","sequence":"first","affiliation":[{"name":"Department of Chemistry Special Research Unit for Advanced Magnetic Resonance Center of Excellence for Innovation in Chemistry Faculty of Science Kasetsart University Bangkok 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