Honzatko R B, Monaco H L, Lipscomb W N
Proc Natl Acad Sci U S A. 1979 Oct;76(10):5105-9. doi: 10.1073/pnas.76.10.5105.
The binding sites of CTP, CDP, 5-BrCTP, and ATP to the allosteric site of aspartate carbamoyltransferase (carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) have been found in electron-density maps obtained at about 3 A resolution from x-ray diffraction studies of single crystals. The activator ATP binds in the anti conformation, whereas the inhibitor 5-BrCTP binds in the syn conformation. Both activator and inhibitor bind to the same local region of the enzyme. All of the cytidine nucleotides show important interactions of the base with the protein. The triphosphate conformations are similar, whereas the terminal phosphate of CDP occupies the site of the gamma-phosphate of CTP, thus implying a protein-nucleotide interaction at this site. These results are then related to biochemical studies.
通过对单晶进行X射线衍射研究,在分辨率约为3埃的电子密度图中发现了CTP、CDP、5-BrCTP和ATP与天冬氨酸氨甲酰基转移酶(氨甲酰磷酸:L-天冬氨酸氨甲酰基转移酶,EC 2.1.3.2)变构位点的结合位点。激活剂ATP以反式构象结合,而抑制剂5-BrCTP以顺式构象结合。激活剂和抑制剂都结合到酶的同一局部区域。所有胞苷核苷酸都显示出碱基与蛋白质的重要相互作用。三磷酸的构象相似,而CDP的末端磷酸占据CTP的γ-磷酸的位点,因此意味着在该位点存在蛋白质-核苷酸相互作用。然后将这些结果与生化研究联系起来。