Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination
文献类型：期刊论文
| 作者 | Liu, YQ; Liao, J; Zhu, B; Wang, ED; Ding, JP; Liu, YQ; Liao, J; Zhu, B; Wang, ED; Ding, JP |
| 刊名 | BIOCHEMICAL JOURNAL
 |
| 出版日期 | 2006 |
| 卷号 | 394期号:1页码:399-407 |
| 关键词 | aminoacyl-tRNA synthetase aminoacylation editing domain lock-and-key mechanism recognition |
| 通讯作者 | Ding, JP (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Key Lab Prot, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,jpding@sibs.ac.cn |
| 英文摘要 | aaRSs (aminoacyl-tRNA synthetases) are responsible for the covalent linking of amino acids to their cognate tRNAs via the aminoacylation reaction and play a vital role in maintaining the fidelity of protein synthesis. LeuRS (leucyl-tRNA synthetase) can link not only the cognate leucine but also the nearly cognate residues Ile and Met to tRNA(Leu). The editing domain of LeuRS deacylates the mischarged Ile-tRNA(Leu) and Met-tRNA(Leu). We report here the crystal structures of ecLeuRS-ED (the editing domain of Escherichia coli LeuRS) in both the apo form and in complexes with Met and Ile at 2.0 angstrom, 2.4 angstrom, and 3.2 angstrom resolution respectively. The editing active site consists of a number of conserved amino acids, which are involved in the precise recognition and binding of the noncognate amino acids. The substrate-binding pocket has a rigid structure which has an optimal stereochemical fit for Ile and Met, but has steric hindrance for leucine. Based on our structural results and previously available biochemical data, we propose that ecLeuRS-ED uses a lock-and-key mechanism to recognize and discriminate between the amino acids. Structural comparison also reveals that all subclass la aaRSs share a conserved structure core consisting of the editing domain and conserved residues at the editing active site, suggesting that these enzymes may use a common mechanism for the editing function. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | CP1 DOMAIN ; L-VALINE ; AMINOACYLATION ; ISOLEUCINE ; THREONINE ; ERRORS ; YEAST ; SITE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000235723700004 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1833]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Liu, YQ,Liao, J,Zhu, B,et al. Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination[J]. BIOCHEMICAL JOURNAL,2006,394(1):399-407. |
| APA | Liu, YQ.,Liao, J.,Zhu, B.,Wang, ED.,Ding, JP.,...&Ding, JP.(2006).Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination.BIOCHEMICAL JOURNAL,394(1),399-407. |
| MLA | Liu, YQ,et al."Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination".BIOCHEMICAL JOURNAL 394.1(2006):399-407. |
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