CRYSTAL STRUCTURE OF VP55-VP39 HETERODIMER WITH A SHORT OLIGO

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 我们的魅力是牛痘病毒聚（A）聚合酶（VP 55）的结构和分子动力学-已知唯一的非模板RNA聚合酶易位相对于其RNA引物。它有一个持续合成因子（VP 39），可以改变易位模式。过去，合作研究产生了VP 55与VP 39复合的晶体结构。目前，最重要但不完整的结构信息涉及VP 55-VP 39-RNA复合物。 最近，用短RNA片段和ATP浸泡表征良好的晶体提供了令人兴奋的初步数据。然而，我们目前较低的分辨率（3.36 <$）阻碍了我们对多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来完全解析引物和NTP的催化复合物。

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.