Raskar, T. orcid.org/0000-0001-7188-7428, Niebling, S. orcid.org/0000-0001-6582-5984, Devos, J.M. orcid.org/0000-0001-5989-6794 et al. (6 more authors) (2022) Structure and diffusive dynamics of aspartate α-decarboxylase (ADC) liganded with d-serine in aqueous solution. Physical Chemistry Chemical Physics, 24 (34). pp. 20336-20347. ISSN 1463-9076
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © the Owner Societies 2022. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. |
Keywords: | Escherichia coli; Carboxy-Lyases; Aspartic Acid; Serine; Ligands; Diffusion; Models, Molecular |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Physical Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 17 Jul 2023 10:51 |
Last Modified: | 17 Jul 2023 10:51 |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/d2cp02063g |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:201579 |