STRUCTURAL STUDIES OF DNA RECOMBINASES AND INDIRECT RECOGNITION OF DNA SEQUENCE

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。 DNA识别和重组的结构研究 我们的研究重点是DNA重组反应的结构理解。 对于我们研究的几种酶（Rad 51，Flp和Sin），我们已经确定了初始结构，现在正在通过额外的结构和生物化学研究对其机制进行更深入的了解。 例如，对于丝氨酸重组酶Sin，我们希望确定与不同结合位点结合的蛋白质的结构以及酶正常发挥功能的大型多蛋白复合物的结构。 对于另一个项目，来自噬菌体mu的转座酶，我们有最终转座复合物的晶体（4 ~ 60 kDa的原聚体加上135 bp的DNA），其分辨率适中，但我们需要更多更好的数据来解决相位问题。 这将是任何DNA转座酶的产物复合物的第一个结构。 最后，我们还研究了E. coli SOS反应调节因子莱克萨与DNA的融合。

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. Structural studies of DNA recognition & recombination Our research focuses on the structural understanding of DNA recombination reactions. For several of the enzymes we study (Rad51, Flp, and Sin) we have determined initial structures and are now working towards a deeper understanding of their mechanism through additional structural and biochemical studies. For example, for the serine recombinase Sin, we hope to determine the structures of the protein bound to different binding sites and of the large multi-protein complex within which the enzyme normally functions. For another project, the transposase from phage mu, we have crystals of the final transposition complex (4 ~60kDa protomers plus 135bp of DNA) that diffract to modest resolution, but we need more and better data to solve the phase problem. This would be the first structure of a product complex for any DNA transposase. Finally, we are also studying the interactions of the E. coli SOS response regulator LexA with DNA.