SCHIMMEL PRT-CRYSTAL STRUCTURE OF TRBP111/TRNA COMPLEX

TRBP111/TRNA 复合物的 SCHIMMEL PRT 晶体结构

• 批准号: 8362037
• 负责人: PAUL R SCHIMMEL
• 金额: $ 0.19万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362037
• 关键词: Amino Acyl-tRNA Synthetases; Aminoacylation; Apoptosis; Complex; Data; Databases; Enzymes; Equipment; Escherichia coli; Funding; Genomics; Grant; Housing; Human; National Center for Research Resources; Nature; Principal Investigator; Protein Biosynthesis; RNA; Radiation; Research; Research Infrastructure; Resolution; Resources; Roentgen Rays; Shapes; Source; Structure; Transfer RNA; United States National Institutes of Health; cost; cytokine; dimer; interest; novel; receptor; structural biology

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Trbp111 is an ancient, structure-specific tRNA recognition domain found in many novel, human apoptosis-related cytokines, aminoacyl-tRNA synthetases, and other components of the protein synthesis apparatus. The function of this domain is to recognize the general L-shape of tRNA, regardless of sequence, and deliver it to its receptor enzyme for efficient aminoacylation. I want to understand the nature of this structure-specific tRNA recognition at an atomic level. Therefore, I determined the crystal structure of bacterial Trbp111 which revealed a homodimer with two OB-fold domains and a novel dimer interface (Swairjo et al., EMBO J, 19: 6287, 2000). I am now pursuing the crystal structure of the complex with tRNA. I have produced crystals of Aquifex aeolicus Trbp111 complexed with E. coli tRNAfMet which diffract to 7.0 ¿ on in-house equipment. I hope to collect higher-resolution X-ray data at SSRL that would allow for determination of the complex structure. This project is part of our general interest in studying several, novel, non-specific RNA recognition domains identified recently in genomic databases (Avarind and Koonin, J. Mol. Evol., 38: 291, 1999).

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 TRBP111是在许多小说中发现的一个古老的，结构特异性的tRNA识别域，与人凋亡相关的细胞因子，氨基酰基-TRNA合成酶以及蛋白质合成设备的其他成分。该结构域的功能是识别tRNA的一般L形，无论序列如何，并将其输送到其受体酶以进行有效的氨基酰化。我想了解原子水平上这种特定于结构的tRNA识别的性质。因此，我确定了细菌TRBP111的晶体结构，该晶体结构揭示了一个具有两个OB折叠域和一个新型二聚体界面的同型二聚体（Swairjo等，Embo J，19：6287，2000）。我现在正在用tRNA追求复合物的晶体结构。我已经生产了Aquifex aeolicus trbp111的晶体，该晶体与大肠杆菌trnafmet复合，在内部设备上衍射为7.0。我希望在SSRL上收集高分辨率的X射线数据，以确定复杂的结构。该项目是我们在基因组数据库中发现的几个新型，非特异性RNA识别域的普遍兴趣的一部分（Avarind和Koonin，J。Mol。Evol。，38：291，1999）。