Solution structure of the ribosome recycling factor from Aquifex aeolicus.
Solution structure of the ribosome recycling factor from Aquifex aeolicus.
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DOI：
10.1021/bi002474g
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发表时间：
2001-02
期刊：
影响因子：
2.9
通讯作者：
T. Yoshida;S. Uchiyama;H. Nakano;H. Kashimori;H. Kijima;T. Ohshima;Y. Saihara;T. Ishino;H. Shimahara;T. Yoshida;K. Yokose;T. Ohkubo;A. Kaji;Y. Kobayashi
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文献类型：
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作者：
T. Yoshida;S. Uchiyama;H. Nakano;H. Kashimori;H. Kijima;T. Ohshima;Y. Saihara;T. Ishino;H. Shimahara;T. Yoshida;K. Yokose;T. Ohkubo;A. Kaji;Y. Kobayashi
利用异谱多维核磁共振技术研究了超嗜热菌风产液菌核糖体再循环因子（RRF）的溶液结构。使用NOE、J耦合和T1/T2各向异性的限制计算了15种结构。所得结构具有两个结构域的整体L形构象，与tRNA分子相似。结构域I（对应于tRNA的反密码子茎）是一个刚性的三个α-螺旋束。与通常的卷曲螺旋排列略有不同，结构域I的每个螺旋不是扭曲的，而是直的，平行于主轴。结构域II（对应于tRNA的CCA末端部分）是具有α-螺旋和两个β-折叠的α/β结构域，其具有一些柔性区域。当分别计算时，两个结构域的骨架原子均方根偏差（rmsd）值为0.7 A，其小于分子整体的骨架原子均方根偏差（rmsd）值（1.4 A）。15 N-[1H] NOE值的测量表明，L形分子角上的残基正在进行快速的内部运动。这些结果表明，两个畴之间的连接区域有助于两个畴的取向的波动。因此，表明RRF在其起作用的溶液中保持tRNA模拟。
The solution structure of ribosome recycling factor (RRF) from hyperthermophilic bacterium, Aquifex aeolicus, was determined by heteronuclear multidimensional NMR spectroscopy. Fifteen structures were calculated using restraints derived from NOE, J-coupling, and T1/T2 anisotropies. The resulting structure has an overall L-shaped conformation with two domains and is similar to that of a tRNA molecule. The domain I (corresponding to the anticodon stem of tRNA) is a rigid three alpha-helix bundle. Being slightly different from usual coiled-coil arrangements, each helix of domain I is not twisted but straight and parallel to the main axis. The domain II (corresponding to the portion with the CCA end of tRNA) is an alpha/beta domain with an alpha-helix and two beta-sheets, that has some flexible regions. The backbone atomic root-mean-square deviation (rmsd) values of both domains were 0.7 A when calculated separately, which is smaller than that of the molecule as a whole (1.4 A). Measurement of 15N-[1H] NOE values show that the residues in the corner of the L-shaped molecule are undergoing fast internal motion. These results indicate that the joint region between two domains contributes to the fluctuation in the orientation of two domains. Thus, it was shown that RRF remains the tRNA mimicry in solution where it functions.