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首页> 外文期刊>Journal of Molecular Biology >SOLUTION STRUCTURE OF THE ANTICODON-BINDING DOMAIN OF ESCHERICHIA COLI LYSYL-TRNA SYNTHETASE AND STUDIES OF ITS INTERACTION WITH TRNA(LYS)
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SOLUTION STRUCTURE OF THE ANTICODON-BINDING DOMAIN OF ESCHERICHIA COLI LYSYL-TRNA SYNTHETASE AND STUDIES OF ITS INTERACTION WITH TRNA(LYS)

机译：大肠埃希氏菌赖氨酸-TRNA合成酶抗原结合域的溶液结构及其与TRNA（LYS）相互作用的研究

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摘要

A protein domain corresponding to residues 31 to 149 of the E. coli Lysyl-tRNA synthetase species corresponding to the lysS gene was expressed and N-15-labelled. H-1 and N-15 NMR resonance assignments for this domain were obtained by two-dimensional and three-dimensional homonuclear and heteronuclear spectroscopy. Using distance geometry and simulated annealing, a three-dimensional structure could be calculated using 701 NOE and 86 dihedral angle restraints. It is composed of a five-stranded antiparallel beta-barrel capped by three alpha-helices at its ends. This structure closely resembles that of the N-terminal domain of the other E. coli lysyl-tRNA synthetase species expressed from the lysU gene and is highly homologous to the fold observed for the corresponding region of aspartyl-tRNA synthetase. It is shown that the isolated N-terminal fragment of lysyl-tRNA synthetase can interact with tRNA(Lys) as well as with poly (U), which mimics the anticodon sequence. Amino acid residues involved in these interactions were identified and, in the case of poly-U, a number of specific protein-RNA contacts were characterized. Specific recognition of tRNA(Lys) involves a cluster of four structurally well-defined aromatic residues, anchored on the beta-strands, and basic residues located on the surrounding loops. This organization is reminiscent of other RNA binding proteins, such as the U1A small nuclear ribonucleoprotein. (C) 1995 Academic Press Limited [References: 55]
机译：表达对应于lysS基因的大肠杆菌Lysyl-tRNA合成酶种类的残基31至149的蛋白质结构域并进行N-15标记。该域的H-1和N-15 NMR共振分配是通过二维和三维同核和异核光谱获得的。使用距离几何结构和模拟退火，可以使用701 NOE和86二面角约束来计算三维结构。它是由一个五链反平行β枪管组成，在其末端被三个α螺旋覆盖。该结构与从lysU基因表达的其他大肠杆菌lysyl-tRNA合成酶物种的N端结构域非常相似，并且与天冬氨酰tRNA合成酶相应区域的折叠高度同源。结果表明，赖氨酰-tRNA合成酶的分离的N-末端片段可以与tRNA（Lys）以及与模拟反密码子序列的poly（U）相互作用。鉴定了参与这些相互作用的氨基酸残基，在poly-U的情况下，鉴定了许多特定的蛋白质-RNA接触。 tRNA（Lys）的特异性识别涉及由四个结构明确的芳香族残基组成的簇，锚定在β链上，碱性残基位于周围的环上。这种组织使人联想到其他RNA结合蛋白，例如U1A小核糖核糖核蛋白。 （C）1995 Academic Press Limited [参考号：55]

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