STRUCTURAL STUDIES ON DNA GYRASE

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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.