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Reverse gyrase zinc finger This is the N-terminal zinc finger domain present in reverse gyrase proteins. Most reverse gyrases have a conserve the N-terminal zinc finger domain adopting a treble clef fold, suggesting the importance of this domain domain for the proteins function. In addition, these proteins contain a second zinc finger of zinc beta-ribbon type that is grafted into the Toprim domain (pfam01751). Deletion of both zinc fingers abolishes supercoiling activity of reverse gyrase. The structure of Thermotoga maritima reverse gyrase shows that the N-terminal zinc finger firmly attaches the H1 (helicase 1) domain to the topoisomerase domain contributing to double-strand DNA (dsDNA) binding. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",