CRYSTAL STRUCTURE OF VP55-VP39 HETERODIMER WITH A SHORT OLIGO

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。 我们着迷的是痘苗病毒聚(A)聚合酶(VP55)的结构和分子动力学--已知的唯一相对于其RNA引物易位的非模板RNA聚合酶。它具有改变易位模式的加工性因子(VP39)。过去，合作研究产生了VP55与VP39络合的晶体结构。目前，关于VP55-VP39-RNA复合体的结构信息最重要，但不完整。最近，用短RNA片段和ATP浸泡特征良好的晶体提供了令人兴奋的初步数据。然而，在这个竞争激烈的领域，我们目前较低的分辨率(3.36？)阻碍了我们对聚腺苷酸化机制的充分理解。我们非常需要稍微高一点的分辨率来完全拆分带有底物和NTP的催化络合物。

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.