Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Bα complex
Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Bα complex
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DOI：
10.1038/88598
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发表时间：
2001-06-01
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影响因子：
--
通讯作者：
Nyborg, J
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文献类型：
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作者：
Andersen, GR;Valente, L;Nyborg, J
在蛋白质生物合成的延伸周期中，核苷酸交换因子eEF1B α催化与g蛋白eEF1A结合的GDP交换GTP。为了获得更多关于最近解决的eEF1A-eF1B α结构的信息，我们分别在3.0,2.4和2.05埃分辨率下测定了eEF1A-eEF1B α -GDP- mg2 +， eif1a - eef1b α -GDP和eEF1A-eEF1B α -GDPNP配合物的结构。eEF1A和eEF1Ba的微小变化，特别是在核苷酸结合位点周围，与体内数据一致。与其他已知的核苷酸g蛋白复合物一样，碱基、糖和磷酸结合，而磷酸和磷酸则是无序的。eEF1B α中的Lys 205突变插入eEF1A的Mg2+结合位点是致命的。这与结构一起强调了Mg2+在eEF1A-eEF1B α复合物中核苷酸交换的重要作用。
In the elongation cycle of protein biosynthesis, the nucleotide exchange factor eEF1B alpha catalyzes the exchange of GDP bound to the G-protein, eEF1A, for GTP. To obtain more information about the recently solved eEF1A-eF1B alpha structure, we determined the structures of the eEF1A-eEF1B alpha -GDP-Mg2+, eEIF1A-eEF1B alpha -GDP and eEF1A-eEF1B alpha -GDPNP complexes at 3.0, 2.4 and 2.05 Angstrom resolution, respectively. Minor changes, specifically around the nucleotide binding site, in eEF1A and eEF1Ba are consistent with in vivo data. The base, sugar and alpha -phosphate bind as in other known nucleotide G-protein complexes, whereas the beta- and gamma -phosphates are disordered. A mutation of Lys 205 in eEF1B alpha that inserts into the Mg2+ binding site of eEF1A is lethal. This together with the structures emphasizes the essential role of Mg2+ in nucleotide exchange in the eEF1A-eEF1B alpha complex.