Institut Max von Laue - Paul Langevin, 71 Avenue des Martyrs, Grenoble 38000, France.
Partnership for Structural Biology, 71 Avenue des Martyrs, Grenoble 38000, France.
Phys Chem Chem Phys. 2022 Aug 31;24(34):20336-20347. doi: 10.1039/d2cp02063g.
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.
非相干中子光谱学与动态光散射相结合，用于研究配体结合对天冬氨酸脱羧酶（ADC）质心自扩散和内部扩散动力学的影响。还确定了 ADC 与 D-丝氨酸抑制剂复合物的 X 射线晶体结构，并使用分子动力学模拟进一步探测由于配体结合而发生的结构重排。这些实验表明，D-丝氨酸与一些活性位点残基形成氢键，ADC 四聚体的更高阶寡聚体在纳秒-毫秒时间尺度上存在，并且还表明配体结合不仅影响 ADC 的内部扩散动力学，而且似乎进一步增加了更高阶寡聚体的大小。
