Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R
European Molecular Biology Laboratory, Grenoble Outstation, France.
Nature. 1996 Feb 8;379(6565):511-8. doi: 10.1038/379511a0.
The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors. The two EF-Ts molecules form a tight dimer, but there is little contact between the two EF-Tu molecules. The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides.
已确定来自大肠杆菌的EF-Tu.EF-Ts复合物的晶体结构，分辨率为2.5埃。该复合物包含每种延伸因子的两个亚基。两个EF-Ts分子形成紧密的二聚体，但两个EF-Tu分子之间几乎没有接触。EF-Ts与EF-Tu的相互作用主要导致Mg2+离子结合位点的破坏，从而降低EF-Tu对鸟嘌呤核苷酸的亲和力。
