Raskar, T, Niebling, S, Devos, JM, Yorke, BA, Härtlein, M, Huse, N, Forsyth, VT ORCID: https://orcid.org/0000-0003-0380-3477, Seydel, T and Pearson, AR (2022) Structure and diffusive dynamics of aspartate α-decarboxylase (ADC) liganded with D-serine in aqueous solution. Physical Chemistry Chemical Physics, 24 (34). 20336 - 20347.

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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.

Item Type: Article
Additional Information: Open Access Article This Open Access Article is licensed under a Creative Commons Attribution 3.0 Unported Licence
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
Divisions: Faculty of Natural Sciences > School of Chemical and Physical Sciences
Related URLs:
Depositing User: Symplectic
Date Deposited: 09 Sep 2022 11:11
Last Modified: 09 Sep 2022 11:11
URI: https://eprints.keele.ac.uk/id/eprint/11390

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