Natural products of the acetate pathway are biosynthesized through the actions of multiple catalytic domains. Intermediates are covalently bound to a small acyl carrier protein (ACP) that stabilizes bound intermediates by sequestering them within its helices and delivers them to catalytic domains through specific protein-protein interactions. We have developed methods to chemo-enzymatically synthesize CoA analogs and append them to ACPs in order to study activity and structure. Recently we have used protein NMR to investigate the molecular details of how ACP recognizes and binds its enzymatic partners and the mechanism by which ACP delivers its cargo from its internal binding pocket into the active sites of the biosynthetic enzymes.

Structure and protein-protein interaction in the acetate pathway

243rd National Meeting (2012)

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