Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation
Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation
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DOI：
10.1016/j.cell.2005.04.015
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发表时间：
2005-07-01
期刊：
影响因子：
64.5
通讯作者：
Wahl, MC
中科院分区：
文献类型：
--
作者：
Diaconu, M;Kothe, U;Wahl, MC
细菌核糖体大亚基的L7/12茎包含蛋白L10和L7/12的多个拷贝。我们目前的晶体结构Thermotoga maritima L10在复杂的三个L7/12 N-末端结构域二聚体，完善的古生菌L10 E N-末端结构域的50 S亚基的结构，并确定这些元素在大肠杆菌核糖体的冷冻电子显微镜重建。L10的移动的C-末端螺旋α 8在海栖热蜱中携带三个L7/12二聚体，在大肠杆菌中携带两个。大肠杆菌中，与这些生物体中L10的螺旋α 8的不同长度一致。茎被组织成三个元件（茎基部、L10螺旋α 8-L7/12 N-末端结构域复合物和L7/12 C-末端结构域），它们通过柔性连接而连接。高度移动的L7/12 C-末端结构域促进翻译因子向核糖体的募集，并通过稳定其活性GTP酶构象刺激核糖体结合因子对GTP的水解。
The L7/12 stalk of the large subunit of bacterial ribosomes encompasses protein L10 and multiple copies of L7/12. We present crystal structures of Thermotoga maritima L10 in complex with three L7/12 N-terminaldomain dimers, refine the structure of an archaeal L10E N-terminal domain on the 50S subunit, and identify these elements in cryo-electron-microscopic reconstructions of Escherichia coli ribosomes. The mobile C-terminal helix alpha 8 of L10 carries three L7/12 dimers in T maritima and two in E. coli, in concordance with the different length of helix alpha 8 of L10 in these organisms. The stalk is organized into three elements (stalk base, L10 helix alpha 8-L7/12 N-terminaldomain complex, and L7/12 C-terminal domains) linked by flexible connections. Highly mobile L7/12 C-terminal domains promote recruitment of translation factors to the ribosome and stimulate GTP hydrolysis by the ribosome bound factors through stabilization of their active GTPase conformation.