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- W2912978911 abstract "Engineering carrier protein dependent pathways relies upon a thorough understanding of the molecular basis of carrier protein-partner enzyme interactions. AcpP, the acyl carrier protein involved in Escherichia coli fatty acid biosynthesis, delivers a vast array of substrates to the appropriate partner enzyme, efficiently distinguishing between at least 21 different enzymes in both primary and secondary metabolic pathways. Fatty acyl substrates are covalently tethered to the AcpP and at the same time sequestered inside a hydrophobic cavity of the protein, leading to an allosteric modification of the AcpP surface that participates in a transient binding event. Here, the substrate is flipped out of the AcpP pocket and into the active site of the enzyme. Due to the complexity of this interaction, it has been difficult to delineate the mechanisms used by AcpP to convey substrate identity to partner enzymes. Herein, we provide a detailed description of how AcpP structure is effected by sequestration of various substrates by combining nuclear magnetic resonance spectroscopy with molecular dynamics simulations. Additionally, we investigate the interaction of AcpP with enzymes from fatty acid biosynthesis and secondary metabolic pathways. These findings elucidate information on carrier protein substrate shuttling, which, taken with previous data will facilitate rational design of carrier protein-partner enzyme complexes." @default.
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- W2912978911 date "2019-02-01" @default.
- W2912978911 modified "2023-09-30" @default.
- W2912978911 title "Computational and Spectroscopic Investigation of Communication Mechanisms used by Acyl Carrier Proteins" @default.
- W2912978911 doi "https://doi.org/10.1016/j.bpj.2018.11.1035" @default.
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