Modular type I polyketide synthase acyl carrier protein domains share a common N-terminally extended fold.

ABSTRACT: Acyl carrier protein (ACP) domains act as interaction hubs within modular polyketide synthase (PKS) systems, employing specific protein-protein interactions to present acyl substrates to a series of enzyme active sites. Many domains from the multimodular PKS that generates the toxin mycolactone display an unusually high degree of sequence similarity, implying that the few sites which vary may do so for functional reasons. When domain boundaries based on prior studies were used to prepare two isolated ACP segments from this system for studies of their interaction properties, one fragment adopted the expected tertiary structure, but the other failed to fold, despite sharing a sequence identity of 49%. Secondary structure prediction uncovered a previously undetected helical region (H0) that p

SUBMITTER: Moretto L 

PROVIDER: S-EPMC6382882 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature