SCHIMMEL PRT-CRYSTAL STRUCTURE OF TRBP111/TRNA COMPLEX

TRBP111/TRNA 复合物的 SCHIMMEL PRT 晶体结构

• 批准号: 7721746
• 负责人: PAUL R SCHIMMEL
• 金额: $ 0.15万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721746
• 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).

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 Trbp111是一个古老的、结构特异的tRNA识别结构域，存在于许多新的人类凋亡相关细胞因子、氨酰-tRNA合成酶和其他蛋白质合成装置的成分中。这个结构域的功能是识别tRNA的一般L形状，无论其序列如何，并将其运送到其受体酶进行有效的氨基酰化。我想在原子水平上了解这种结构特异性tRNA识别的性质。因此，我测定了细菌Trbp111的晶体结构，发现了一个具有两个OB-折叠结构域的同源二聚体和一个新的二聚体界面(Swirjo等人，EMBO J，19：6287,2000)。我现在正在用tRNA研究这个复合体的晶体结构。我已经在内部设备上生产了与大肠杆菌tRNAfMet络合的Aquifex aeolicus Trbp111晶体，衍射率为7.0。我希望在SSRL收集更高分辨率的X射线数据，以便确定复杂的结构。这个项目是我们研究最近在基因组数据库中发现的几个新的、非特定的RNA识别结构域的普遍兴趣的一部分(Avarind和Koning，J.Mol。事件，38：291,1999)。