SCHIMMEL PRT-CRYSTAL STRUCTURE OF TRBP111/TRNA COMPLEX

TRBP111/TRNA 复合物的 SCHIMMEL PRT 晶体结构

• 批准号: 8169909
• 负责人: PAUL R SCHIMMEL
• 金额: $ 0.2万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169909
• 关键词: Amino Acyl-tRNA Synthetases; Aminoacylation; Apoptosis; Complex; Computer Retrieval of Information on Scientific Projects Database; Data; Databases; Enzymes; Equipment; Escherichia coli; Funding; Genomics; Grant; Housing; Human; Institution; Nature; Protein Biosynthesis; RNA; Research; Research Personnel; Resolution; Resources; Roentgen Rays; Shapes; Source; Structure; Transfer RNA; United States National Institutes of Health; cytokine; dimer; interest; novel; receptor

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 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).

该副本是使用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这是调查员的机构。 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）。