Structural and Dynamic Insights into Acyl Carrier Protein upon Metal Binding and Acylation Revealed by NMR Spectroscopy and MD Simulations.

ABSTRACT: Protein dynamics are crucial for the acyl carrier protein (ACP) acting as a cofactor, communicating with various fatty acid synthesis (FAS) enzymes. Using a combination of NMR spectroscopy and molecular dynamics (MD) simulations, we demonstrate how the conformational flexibility of Escherichia coli ACP (EcACP) modulates metal binding and facilitates its molecular switches, thereby determining the pathway for different acyl chains. Our results show that Ca²⁺ binding greatly stabilizes the protein-boosting thermal stability by over 13 °C-and modulates its dynamic properties, affecting two acidic metal binding sites and the conformation of the hydrophobic cavity. Hydrogen-deuterium exchange and chemical denaturation experiments revealed that Ile11 and Ile72 are the ke

SUBMITTER: Lee CY 

PROVIDER: S-EPMC12469350 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature