Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bα
Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bα
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DOI：
10.1016/s1097-2765(00)00122-2
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发表时间：
2000-11-01
期刊：
影响因子：
16
通讯作者：
Nyborg, J
中科院分区：
文献类型：
--
作者：
Andersen, GR;Pedersen, L;Nyborg, J
蛋白质生物合成延伸因子eEF 1A（以前称为EF-1 α）和其交换因子eEF 1B α（以前称为EF-1 β）的催化C末端之间的复合物的晶体结构被确定为1.67埃分辨率。核苷酸交换因子的一端被掩埋在eEF 1A的开关1和2区域之间，并破坏与核苷酸相关的Mg 2+离子的结合位点。eEF 1B alpha的第二末端与eEF 1A的结构域2相互作用，该区域被假设参与tRNA的CCA-氨酰基末端的结合。eEF 1B α和氨酰化tRNA之间的竞争可能是真核生物蛋白质合成中引导反应物的核心要素。eEF 1B α对eEF 1A的识别与在原核EF-Tu：EF-Ts复合物中观察到的非常不同。然而，在核苷酸交换中开关2区域的识别对于延伸因子复合物以及Ras：Sos和Arf 1：Sec 7的复合物是常见的。
The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1 alpha) and the catalytic C terminus of its exchange factor, eEF1B alpha (formerly EF-1 beta), was determined to 1.67 Angstrom resolution. One end of the nucleotide exchange factor is buried between the switch 1 and 2 regions of eEF1A and destroys the binding site for the Mg2+ ion associated with the nucleotide. The second end of eEF1B alpha interacts with domain 2 of eEF1A in the region hypothesized to be involved in the binding of the CCA-aminoacyl end of the tRNA. The competition between eEF1B alpha and aminoacylated tRNA may be a central element in channeling the reactants in eukaryotic protein synthesis. The recognition of eEF1A by eEF1B alpha is very different from that observed in the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in nucleotide exchange is, however, common to the elongation factor complexes and those of Ras:Sos and Arf1:Sec7.