Solution structure of human initiation factor eIF2α reveals homology to the elongation factor eEF1B
Solution structure of human initiation factor eIF2α reveals homology to the elongation factor eEF1B
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DOI：
10.1016/j.str.2004.07.010
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发表时间：
2004-09-01
期刊：
影响因子：
5.7
通讯作者：
Wagner, G
中科院分区：
文献类型：
--
作者：
Ito, T;Marintchev, A;Wagner, G
GTP结合形式的三聚体真核生物翻译起始因子2（eIF 2）将氨酰化的起始剂甲硫氨酰tRNA转移到40 S核糖体上。我们已经解决了与解决NMR的结构的a亚基的人eIF 2（heIF 2alpha）。该蛋白质由两个相对于彼此可移动的结构域组成。N-末端结构域具有SI型寡核苷酸/寡糖结合折叠亚结构域和α-螺旋亚结构域。C-末端结构域采用与延伸因子（eEF）1B α（eEF 1A的鸟嘌呤核苷酸交换因子）的C-末端结构域非常相似的α-折叠。eIF 2 alpha/eIF 2 gamma和eEF 1B alpha/eEF 1A之间的结构和功能相似性表明eIF 2 alpha与eIF 2 gamma以及eIF 2与Met-tRNA（i）（Met）相互作用的模型。它进一步表明了以前未被认识的eIF 2 α/γ从功能相关的延伸因子eEF 1B α/eEF 1A复合物的进化谱系。
The GTP-bound form of the trimeric eukaryotic translation initiation factor 2 (eIF2) transfers aminoacylated initiator methionyl tRNA onto the 40S ribosome. We have solved with solution NMR the structure of the a subunit of human eIF2 (heIF2alpha). The protein consists of two domains that are mobile relative to each other. The N-terminal domain has an SI-type oligonucleotide/oligosaccharide binding-fold subdomain and an alpha-helical subdomain. The C-terminal domain adopts an alphabeta-fold very similar to the C-terminal domain of elongation factor (eEF) 1Balpha, the guanine-nucleotide exchange factor for eEF1A. The structural and functional similarities found between eIF2alpha/eIF2gamma and eEF1Balpha/eEF1A suggest a model for the interaction of eIF2alpha with eIF2gamma, and eIF2 with Met-tRNA(i)(Met). It further indicates a previously unrecognized evolutionary lineage of eIF2alpha/gamma from the functionally related elongation factor eEF1Balpha/eEF1A complex.