Ontology highlight
ABSTRACT:
SUBMITTER: Meinke JL
PROVIDER: S-EPMC7102495 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Meinke Jessica L JL Simon Anna J AJ Wagner Drew T DT Morrow Barrett R BR You Shaochen S Ellington Andrew D AD Keatinge-Clay Adrian T AT
ACS synthetic biology 20190912 9
The proteins of <i>trans</i>-acyltransferase modular polyketide synthases (PKSs) self-organize into assembly lines, enabling the multienzyme biosynthesis of complex organic molecules. Docking domains comprised of ∼25 residues at the C- and N-termini of these polypeptides (<sup>C</sup>DDs and <sup>N</sup>DDs) help drive this association through the formation of four-helix bundles. Molecular connectors like these are desired in synthetic contexts, such as artificial biocatalytic systems and biomat ...[more]