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Publication Abstract from PubMed

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 alpha-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.

Structure and diffusive dynamics of aspartate alpha-decarboxylase (ADC) liganded with D-serine in aqueous solution.,Raskar T, Niebling S, Devos JM, Yorke BA, Hartlein M, Huse N, Forsyth VT, Seydel T, Pearson AR Phys Chem Chem Phys. 2022 Aug 31;24(34):20336-20347. doi: 10.1039/d2cp02063g. PMID:35980136^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.