SCHIMMEL PRT-CRYSTAL STRUCTURE OF TRBP111/TRNA COMPLEX

该子项目是利用资源的许多研究子项目之一 由NIH/NCRR资助的中心赠款提供。次级项目的主要支助 子项目的主要研究者可能是由其他来源提供的， 包括其他NIH来源。 为子项目列出的总成本可能 表示子项目使用的中心基础设施的估计数量， NCRR赠款不直接向子项目或子项目工作人员提供资金。 Trbp 111是一个古老的、结构特异性的tRNA识别结构域，存在于许多新的、人类乳腺癌相关的细胞因子、氨酰-tRNA合成酶和蛋白质合成装置的其他组分中。该结构域的功能是识别tRNA的一般L-形状，而不管序列如何，并将其递送至其受体酶以进行有效的氨酰化。我想在原子水平上了解这种结构特异性tRNA识别的本质。因此，我确定了细菌Trbp 111的晶体结构，其揭示了具有两个OB折叠结构域和新的二聚体界面的同源二聚体（Swairjo等人，EMBO J，19：6287，2000）。我现在正在研究与tRNA复合的晶体结构。我已经制备了与E.大肠杆菌tRNAfMet，其在内部设备上的作用为7.0？。我希望在SSRL收集更高分辨率的X射线数据，以确定复杂的结构。该项目是我们研究最近在基因组数据库中鉴定的几种新型非特异性RNA识别结构域的一般兴趣的一部分（Avarind和Koonin，J. Mol. Biol. Evol.，38：291，1999）。

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).