Structure and diffusive dynamics of aspartate α-decarboxylase (ADC) liganded with d-serine in aqueous solution?

Physical Chemistry Chemical Physics Pub Date: 2022-08-11 DOI: 10.1039/D2CP02063G

Abstract

Incoherent neutron spectroscopy, in combination with dynamic light scattering, was used to investigate the effect of ligand binding on the center-of-mass self-diffusion and internal diffusive dynamics of Escherichia coli aspartate α-decarboxylase (ADC). The X-ray crystal structure of ADC in complex with the D-serine inhibitor was also determined, and molecular dynamics simulations were used to further probe the structural rearrangements that occur as a result of ligand binding. These experiments reveal that D-serine forms hydrogen bonds with some of the active site residues, that higher order oligomers of the ADC tetramer exist on ns–ms time-scales, and also show that ligand binding both affects the ADC internal diffusive dynamics and appears to further increase the size of the higher order oligomers.

Graphical abstract: Structure and diffusive dynamics of aspartate α-decarboxylase (ADC) liganded with d-serine in aqueous solution
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