Molecular basis for acyl carrier protein–ketoreductase interaction in <i>trans</i>-acyltransferase polyketide synthases
Munro Passmore, Angelo Gallo, Józef R. Lewandowski, Matthew Jenner
Abstract
-AT PKSs were found to be specific for their cognate partner, indicating highly optimised interaction interfaces driven by evolutionary processes. Using detailed knowledge of the ACP:KR interaction epitope, an ACP domain was engineered to interact with a non-cognate KR domain partner. The results provide novel, high resolution insights into the ACP:KR interface and offer valuable rules for future engineering efforts of biosynthetic assembly lines.
Topics & Concepts
AcyltransferaseAcyl carrier proteinDocking (animal)Protein–protein interactionPolyketide synthasePolyketideChemistryMutagenesisProtein engineeringComputational biologyStereochemistryBiochemistryBiosynthesisBiologyEnzymeMutationGeneNursingMedicineMicrobial Natural Products and BiosynthesisEnzyme Production and CharacterizationMarine Sponges and Natural Products