7A8Y
X-ray crystal structure of Aspartate alpha-decarboxylase in complex with D-Serine
This is a non-PDB format compatible entry.
Summary for 7A8Y
| Entry DOI | 10.2210/pdb7a8y/pdb |
| Descriptor | Aspartate 1-decarboxylase, D-SERINE, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | decarboxylase, lyase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 27034.32 |
| Authors | Yorke, B.A.,Raskar, T. (deposition date: 2020-08-31, release date: 2021-10-06, Last modification date: 2024-11-06) |
| Primary citation | Raskar, T.,Niebling, S.,Devos, J.M.,Yorke, B.A.,Hartlein, M.,Huse, N.,Forsyth, V.T.,Seydel, T.,Pearson, A.R. Structure and diffusive dynamics of aspartate alpha-decarboxylase (ADC) liganded with D-serine in aqueous solution. Phys Chem Chem Phys, 2022 Cited by PubMed 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 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. PubMed: 35980136DOI: 10.1039/d2cp02063g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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