THE CRYSTAL-STRUCTURE OF ELONGATION-FACTOR-G COMPLEXED WITH GDP, AT 2.7-ANGSTROM RESOLUTION
THE CRYSTAL-STRUCTURE OF ELONGATION-FACTOR-G COMPLEXED WITH GDP, AT 2.7-ANGSTROM RESOLUTION
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DOI：
10.1002/j.1460-2075.1994.tb06675.x
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发表时间：
1994-08-15
期刊：
影响因子：
11.4
通讯作者：
MOORE, PB
中科院分区：
文献类型：
--
作者：
CZWORKOWSKI, J;WANG, J;MOORE, PB
伸长因子G(EF-G)催化细菌中蛋白质合成的转位步骤，与其他细菌伸长因子EF-Tu一样，它是GTP酶超家族的成员。我们测定了嗜热菌EF-G-GDP的晶体结构。它是一个细长的分子，其大的N-末端结构域类似于EF-Tu的G结构域，除了一个90个残基的插入，它覆盖了参与EF-Tu和其他G蛋白的核苷酸交换的表面。EF-G和EF-Tu第二个结构域的三级结构几乎相同，但前两个结构域在EF-G-GDP中的相对位置类似于EF-Tu-GTP，而不是EF-Tu-GDP。EF-G的其余三个结构域看起来像RNA结合域，在EF-Tu中没有对应的结构域。
Elongation factor G (EF-G) catalyzes the translocation step of protein synthesis in bacteria, and like the other bacterial elongation factor, EF-Tu-whose structure is already known-it is a member of the GTPase superfamily. We have determined the crystal structure of EF-G-GDP from Thermus thermophilus. It is an elongated molecule whose large, N-terminal domain resembles the G domain of EF-Tu, except for a 90 residue insert, which covers a surface that is involved in nucleotide exchange in EF-Tu and other G proteins. The tertiary structures of the second domains of EF-G and EF-Tu are nearly identical, but the relative placement of the first two domains in EF-G-GDP resembles that seen in EF-Tu-GTP, not EF-Tu-GDP. The remaining three domains of EF-G look like RNA binding domains, and have no counterparts in EF-Tu.