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I24-Microfocus Macromolecular Crystallography	Structure and diffusive dynamics of Aspartate α-decarboxylase (ADC) liganded with D-Serine in aqueous solution Tushar Raskar , Stephan Niebling , Juliette M. Devos , Briony A. Yorke , Michael Haertlein , Nils Huse , V. Trevor Forsyth , Tilo Seydel , Arwen R. Pearson Physical Chemistry Chemical Physics DOI: 10.1039/D2CP02063G Diamond Proposal Number(s): [6386] Open Access Show Abstract ▼ 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.	Aug 2022

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