Ontology highlight
ABSTRACT:
SUBMITTER: Thiele GAR
PROVIDER: S-EPMC5590888 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
Thiele Grace A R GAR Friedman Connie P CP Tsai Kathleen J S KJS Beld Joris J Londergan Casey H CH Charkoudian Louise K LK
Biochemistry 20170508 20
Acyl carrier proteins (ACPs) are central hubs in polyketide and fatty acid biosynthetic pathways, but the fast motions of the ACP's phosphopantetheine (Ppant) arm make its conformational dynamics difficult to capture using traditional spectroscopic approaches. Here we report that converting the terminal thiol of Escherichia coli ACP's Ppant arm into a thiocyanate activates this site to form a selective cross-link with the active site cysteine of its partner ketoacyl synthase (FabF). The reaction ...[more]