STRUCTURAL STUDIES ON DNA GYRASE

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。 该项目旨在进一步了解DNA Gyrase如何结合DNA。 生物化学研究表明DNA Gyrase A（E.大肠杆菌和B. burgdorferi，来自Berger Lab at UC Berkeley）缺失了调节结合的关键残基。 制备不同的构建体并结晶以确定DNA结合功能的结构基础。

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. This project aimed to further our understanding of how DNA Gyrase binds DNA. Biochemical studies suggested the original structures of the CTD of DNA Gyrase A (E. coli from Verdine Lab and B. burgdorferi from the Berger Lab at UC Berkeley) were missing residues key in the regulation of binding. Different constructs were made and crystallized to determine the structural underpinning of the DNA binding function.