Hannah R. Manion

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In an effort to uncover the structural motifs and biosynthetic logic of the relatively uncharacterized trans-acyltransferase polyketide synthases, we have begun the dissection of the enigmatic dehydrating bimodules common in these enzymatic assembly lines. We report the 1.98 Å resolution structure of a ketoreductase (KR) from the first half of a type A(More)
Trans-acyltransferase polyketide synthases (trans-AT PKSs) construct biologically active polyketides, such as the antibiotic mupirocin, in an assembly line process catalyzed by collections of enzymatic domains termed modules. Each module of a trans-AT possesses an acyl carrier protein (ACP) and ketosynthase (KS) that, along with a separately-encoded(More)
C-methyltransferases (MTs) from modular polyketide synthase assembly lines are relatively rare and unexplored domains that are responsible for installing α-methyl groups into nascent polyketide backbones. The stage at which these synthase-embedded enzymes operate during polyketide biosynthesis has yet to be conclusively demonstrated. In this work we(More)
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