Macol C P, Tsuruta H, Stec B, Kantrowitz E R
Department of Chemistry, Boston College, Merkert Chemistry Center, Chestnut Hill, Massachusetts 02467, USA.
Nat Struct Biol. 2001 May;8(5):423-6. doi: 10.1038/87582.
Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.
蛋白质功能的调节通常通过别构机制实现，这对正常生理和细胞过程至关重要。尽管已经提出了许多模型来解释配体与别构蛋白和酶的协同结合，但一直缺乏直接的结构支持。在这里，我们结合使用X射线晶体学和溶液中的小角X射线散射，以提供直接的结构证据，即配体与大肠杆菌天冬氨酸转氨甲酰酶六个活性位点之一的结合会诱导从T态到R态的协同结构转变。
