Molecular dynamics of ribosomal elongation factors G and Tu.
Molecular dynamics of ribosomal elongation factors G and Tu.
复制标题
核糖体延伸因子 G 和 Tu 的分子动力学。
DOI：
10.1007/s00249-010-0647-2
复制
发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Trylska,Joanna
中科院分区：
文献类型：
--
作者：
Kulczycka,Katarzyna;Długosz,Maciej;Trylska,Joanna
核糖体上的翻译受外部因素控制。在多肽延长过程中，延长因子EF-Tu和EF-G连续地与细菌核糖体相互作用。EF-Tu结合并将氨酰-tRNA递送到核糖体A位点，EF-G在形成肽键后帮助tRNA在其结合位点之间移位。这些过程是以牺牲GTP为代价的。EF-Tu：tRNA和EF-G具有相似的形状，共享共同的结合位点，并且在与核糖体相互作用时经历大的构象变化。为了表征这两个伸长因子的内部运动，我们使用了25 ns长的全原子分子动力学模拟。我们观察到EF-G结构域III，IV和V和tRNA的EF-Tu：tRNA复合物的流动性增强。EF-Tu：GDP复合物获得了不同于在具有GTP类似物的EF-Tu的晶体结构中发现的配置，显示开关I和II区域中的构象变化。计算的静电特性的延伸因子没有显示出全球的相似性，即使匹配的静电表面补丁被发现周围的域I，接触的核糖体，并在GDP/GTP结合区。
Translation on the ribosome is controlled by external factors. During polypeptide lengthening, elongation factors EF-Tu and EF-G consecutively interact with the bacterial ribosome. EF-Tu binds and delivers an aminoacyl-tRNA to the ribosomal A site and EF-G helps translocate the tRNAs between their binding sites after the peptide bond is formed. These processes occur at the expense of GTP. EF-Tu:tRNA and EF-G are of similar shape, share a common binding site, and undergo large conformational changes on interaction with the ribosome. To characterize the internal motion of these two elongation factors, we used 25 ns long all-atom molecular dynamics simulations. We observed enhanced mobility of EF-G domains III, IV, and V and of tRNA in the EF-Tu:tRNA complex. EF-Tu:GDP complex acquired a configuration different from that found in the crystal structure of EF-Tu with a GTP analogue, showing conformational changes in the switch I and II regions. The calculated electrostatic properties of elongation factors showed no global similarity even though matching electrostatic surface patches were found around the domain I that contacts the ribosome, and in the GDP/GTP binding region.
原核延伸因子 G 的结构和功能
影响因子：
1.2
作者：
A. Gudkov
通讯作者：
A. Gudkov