The structural organization of substrate loading in iterative polyketide synthases

• Published in: Nature chemical biology Vol. 14; no. 5; pp. 474 - 479
• Main Authors: Herbst, Dominik A, Huitt-Roehl, Callie R, Jakob, Roman P, Kravetz, Jacob M, Storm, Philip A, Alley, Jamie R, Townsend, Craig A, Maier, Timm
• Format: Journal Article
• Language: English
• Published: United States Nature Publishing Group 01.05.2018
• Subjects: Acyl carrier protein; Acyl Carrier Protein - chemistry; Ascomycota - metabolism; Biosynthesis; Catalytic Domain; Cross-Linking Reagents - chemistry; Crosslinking; Cryoelectron Microscopy; Crystal structure; Crystallography, X-Ray; Electron microscopy; Escherichia coli - metabolism; Integration; Metabolites; Microorganisms; Pantetheine - chemistry; Phosphorylation; Polyketide Synthases - chemistry; Propionates - chemistry; Protein Conformation; Protein Domains; Protein Multimerization; Reengineering; Secondary metabolites; Stoichiometry; Substrate Specificity; Substrates

Polyketide synthases (PKSs) are microbial multienzymes for the biosynthesis of biologically potent secondary metabolites. Polyketide production is initiated by the loading of a starter unit onto an integral acyl carrier protein (ACP) and its subsequent transfer to the ketosynthase (KS). Initial subs...