CRYSTAL STRUCTURE OF VP55-VP39 HETERODIMER WITH A SHORT OLIGO

具有短寡核苷酸的 VP55-VP39 异二聚体的晶体结构

• 批准号: 7954480
• 负责人: CHANGGONG LI
• 金额: $ 0.17万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-03-01 至 2010-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7954480
• 关键词: Complex; Computer Retrieval of Information on Scientific Projects Database; DNA-Directed RNA Polymerase; Data; Funding; Grant; Institution; Oligonucleotides; Polyadenylation; Polynucleotide Adenylyltransferase; RNA; RNA primers; Research; Research Personnel; Resolution; Resources; Source; Structure; United States National Institutes of Health; Vaccinia virus; molecular dynamics; structural biology; synchrotron radiation

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. Our fascination is with structure and molecular dynamics of vaccinia virus poly(A) polymerase (VP55) - the only non-templated RNA polymerase known to translocate with respect to its RNA primer. It has a processivity factor (VP39) that changes the mode of translocation. Past, collaborative studies yielded a crystal structure for VP55 complexed with VP39. Currently, the most important, yet incomplete structural information regards the VP55-VP39-RNA complex. Soaking of well characterized crystals with short RNA segments and ATP has recently provided exciting preliminary data. However, our current, lower resolution (3.36 ¿) hinders our full understanding of the mechanism of polyadenylation, in this competitive field. We very much need just a little higher resolution to fully resolve the catalytic complex with primer and NTP.

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。 我们的迷恋是对离子病毒聚（A）聚合酶（VP55）的结构和分子动力学 - 唯一已知相对于其RNA引物的易位的非模拟RNA聚合酶。它具有更改易位模式的加工性因子（VP39）。过去的协作研究产生了与VP39复合的VP55的晶体结构。目前，最重要但不完整的结构信息涉及VP55-VP39-RNA复合物。浸泡具有短RNA片段和ATP的良好特征晶体最近提供了令人兴奋的初步数据。但是，我们当前的较低分辨率（3.36？）阻碍了我们在这个竞争性领域中对聚腺苷酸化机制的全面理解。我们非常需要更高的分辨率来完全解决用底漆和NTP的催化复合物。