Kraal B, de Graaf J M, Mesters J R, van Hoof P J, Jacquet E, Parmeggiani A
Department of Biochemistry, Leiden University, The Netherlands.
Eur J Biochem. 1990 Sep 11;192(2):305-9. doi: 10.1111/j.1432-1033.1990.tb19228.x.
EF-Tu is often referred to as a model for guanine-nucleotide-binding regulatory proteins (G-proteins), since X-ray diffraction analysis of its GTP-binding domain shows a detailed location of the 'consensus' amino acid sequences involved in nucleotide binding. Fluoroaluminates are thought to mimick the gamma-phosphate in the GTPase centre on account of their activating effect on a variety of GTP binding proteins. In the case of EF-Tu, we could find no such effects on the basis of at least three independent functional assays. We did notice, however, complicating interactions between free nucleotides, fluoroaluminates and other ligands. By consequence, if indeed AlF4- behaves as a gamma-phosphate analogue in G-proteins, then EF-Tu must have a different GDP/GTP binding site, despite of the conserved consensus sequences.
延伸因子-Tu(EF-Tu)常被视为鸟嘌呤核苷酸结合调节蛋白(G蛋白)的一个模型,因为对其GTP结合结构域的X射线衍射分析显示了参与核苷酸结合的“共有”氨基酸序列的详细位置。由于氟铝酸盐对多种GTP结合蛋白具有激活作用,所以人们认为它们能模拟GTP酶中心的γ-磷酸基团。就EF-Tu而言,基于至少三种独立的功能测定,我们未发现此类效应。然而,我们确实注意到游离核苷酸、氟铝酸盐和其他配体之间存在复杂的相互作用。因此,如果AlF4-在G蛋白中确实表现为γ-磷酸类似物,那么尽管存在保守的共有序列,EF-Tu必定具有不同的GDP/GTP结合位点。