Diffusive dynamics of Aspartate α-decarboxylase (ADC) liganded with D-serine in aqueous solution
Raskar, T.; Niebling, S.; Devos, J. M.; Yorke, B. A.; Härtlein, M.; Huse, N.; Forsyth, T. V.; Seydel, T.; Pearson, A. R.
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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 E.coli aspartate -decarboxylase (ADC). The X-ray crystal structure of the D-serine inhibitor complex with ADC was also determined, and molecular dynamics simulations used to further probe the structural rearrangements that occur as a result of ligand binding. These experiments reveal the existence of higher order oligomers of the ADC tetramer 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.
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