Distinct ligand-binding modes were observed in AMP-PO4-bound FnAPRT compared to its close homolog.
The binding structure indicates significant ligand movement during bacterial APRT reactions, affecting function and efficiency.
Assessment of ligand-induced conformational changes revealed insights into the structural dynamics of FnAPRT.
These findings may enable deeper understanding of enzyme mechanisms and potential targets for antibacterial strategies.
Abstract
The AMP-PO4-bound FnAPRT exhibited distinct ligand-binding modes despite sharing a high sequence similarity with EcAPRT. The structures demonstrated ligand movement during bacterial APRT reactions.