Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.
Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.
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DOI：
10.1093/nar/gku974
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发表时间：
2014-11-10
影响因子：
14.9
通讯作者：
El'skaya AV
中科院分区：
文献类型：
--
作者：
Crepin T;Shalak VF;Yaremchuk AD;Vlasenko DO;McCarthy A;Negrutskii BS;Tukalo MA;El'skaya AV
真核细胞延伸因子eEF 1A在核糖体多肽链延伸期间在GTP-和GDP-结合构象之间转换。eEF 1A *GTP与80 S核糖体A位点的氨酰-tRNA建立复合物。正确的密码子-反密码子识别触发GTP水解，随后eEF 1A *GDP从核糖体上解离。eEF 1A的“GTP”和“GDP”结合构象的结构是未知的。因此，eEF 1A相关的核糖体机制只能通过与细菌同系物EF-Tu类比来预测。在这里，我们报告的第一个晶体结构的哺乳动物eEF 1A 2 *GDP复合物，这表明主要差异的组织的核苷酸结合结构域和分子内运动的eEF 1A相比，EF-Tu。我们的研究结果解释了哺乳动物eEF 1A中的核苷酸交换机制，并表明eEF 1A *GDP从80 S核糖体解离的第一步是GTP水解后观察到的核苷酸结合结构域的旋转。
Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. eEF1A*GTP establishes a complex with the aminoacyl-tRNA in the A site of the 80S ribosome. Correct codon–anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. The structures of both the ‘GTP’- and ‘GDP’-bound conformations of eEF1A are unknown. Thus, the eEF1A-related ribosomal mechanisms were anticipated only by analogy with the bacterial homolog EF-Tu. Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis.
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