Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X‐ray crystallography.
Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X‐ray crystallography.
复制标题
通过 X 射线晶体学研究二磷酸鸟苷与大肠杆菌延伸因子 Tu 结合的结构细节。
作者：
T. Cour;J. Nyborg;S. Thirup;B. Clark
报道了 X 射线晶体学研究得出的二磷酸鸟苷与大肠杆菌延伸因子 Tu 的修饰形式结合的结构细节。参与核苷酸结合的蛋白质元件位于连接 β 链和 α 螺旋的四个环中。这些环对应于一级序列中的区域，与其他原核和真核延伸因子和起始因子 2 相比，这些区域显示出高度的同源性。
Structural details of the guanosine diphosphate binding to a modified form of elongation factor Tu from Escherichia coli, resulting from X‐ray crystallographic studies, are reported. The protein elements that take part in the nucleotide binding are located in four loops connecting beta‐strands with alpha‐helices. These loops correspond to regions in primary sequences which show a high degree of homology when compared with other prokaryotic and eukaryotic elongation factors and initiation factor 2.