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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以出现在其他 CRISP 条目中 列出的机构是。 对于中心来说，它不一定是研究者的机构。 我们着迷于痘苗病毒多聚（A）聚合酶（VP55）的结构和分子动力学，这是唯一已知可相对于其RNA引物易位的非模板化RNA聚合酶，它具有改变聚合模式的持续因子（VP39）。过去的合作研究得出了 VP55 与 VP39 复合物的晶体结构，目前最重要但不完整的结构信息是 VP55-VP39-RNA 复合物。具有短 RNA 片段和 ATP 的良好表征的晶体最近提供了令人兴奋的初步数据，然而，我们目前的较低分辨率 (3.36 ¿) 阻碍了我们对聚腺苷酸化机制的充分理解，在这个竞争激烈的领域，我们非常需要更高的分辨率。分辨率以完全解析引物和 NTP 的催化复合物。