• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Symmetric Assembly of a Decameric Subcomplex in Human Multi-tRNA Synthetase Complex Via Interactions between Glutathione Transferase-Homology Domains and Aspartyl-tRNA Synthetase
【24h】

Symmetric Assembly of a Decameric Subcomplex in Human Multi-tRNA Synthetase Complex Via Interactions between Glutathione Transferase-Homology Domains and Aspartyl-tRNA Synthetase

机译：通过谷胱甘肽转移酶 - 同源域 - 同源域和阿斯巴氨氨酰-TRNA合成酶之间的相互作用对称组装人多重TRNA合成酶复合物中的透明子复合物

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Aminoacyl-tRNA synthetases (AARSs) ligate amino acids to their cognate tRNAs during protein synthesis. In humans, eight AARSs and three non-enzymatic AARS-interacting multifunctional proteins (AIMP1-3), which are involved in various biological processes, form a multi-tRNA synthetase complex (MSC). Elucidation of the structures and multiple functions of individual AARSs and AIMPs has aided current understanding of the structural arrangement of MSC components and their assembly processes. Here, we report the crystal structure of a complex comprising a motif from aspartyl-tRNA synthetase (DRS) and the glutathione transferase (GST)-homology domains of methionyl-tRNA synthetase (MRS), glutamyl-prolyl-tRNA synthetase (EPRS), AIMP2, and AIMP3. In the crystal structure, the four GST domains are assembled in the order of MRS-AIMP3-EPRS-AIMP2, and the GST domain of AIMP2 binds DRS through the beta-sheet in the GST domain. The C-terminus of AIMP3 enhances the binding of DRS to the tetrameric GST complex. A DRS dimer and two GST tetramers binding to the dimer with 2-fold symmetry complete a decameric complex. The formation of this complex enhances the stability of DRS and enables it to retain its reaction intermediate, aspartyl adenylate. Since the catalytic domains of MRS and EPRS are connected to the decameric complex through their flexible linker peptides, and lysyl-tRNA synthetase and AIMP1 are also linked to the complex via the N-terminal region of AIMP2, the DRS-GST tetramer complex functions as a frame in the MSC. (C) 2019 Elsevier Ltd. All rights reserved.
机译：在蛋白质合成期间，氨基酰基-TrNA合成酶（AARS）将氨基酸与其同源TrNA一起连接到其同源TrNAs。在人类中，八个AARS和三种非酶的AARS相互作用的多功能蛋白（AIMP1-3），其参与各种生物方法，形成多重TRNA合成酶复合物（MSC）。阐明各个AARS和旨在的结构和多种功能，对MSC部件及其装配过程的结构布置有助于了解。在这里，我们报告了包含来自阿斯巴氨氨酰-TRNA合成酶（DRS）的基序的晶体结构和甲硫醇-TRNA合成酶（MRS）的谷胱甘肽转移酶（GST）-Shomology结构域，谷氨酸 - 脯氨酰-TRNA合成酶（EPRS）， AIMP2和AIMP3。在晶体结构中，四个GST结构域按照MRS-AIMP3-EPRS-AIMP2组装，AIMP2的GST结构域通过GST结构域中的β-片结合DR。 Aimp3的C-末端增强了DRS与四聚体GST复合物的结合。 DRS二聚体和两种GST四聚体与2倍对称的二聚体结合，完成透冰复合物。该复合物的形成增强了DRS的稳定性，使其能够保留其反应中间体，腺苷腺苷酸。由于MRS和EPRS的催化结构域通过它们的柔性接头肽连接到透明络合物，并且赖氨酰-TRNA合成酶和AIMP1也通过AIMP2的N-末端区域连接到复合物中，DRS-GST四聚体复合物功能MSC中的帧。 （c）2019 Elsevier Ltd.保留所有权利。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号