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- W2068788706 abstract "DNA gyrase, the only topoisomerase able to introduce negative supercoils into DNA, is essential for bacterial transcription and replication; absent from humans, it is a successful target for antibacterials. From biophysical experiments in solution, we report a structural model at ∼12–15 Å resolution of the full-length B subunit (GyrB). Analytical ultracentrifugation shows that GyrB is mainly a nonglobular monomer. Ab initio modeling of small-angle X-ray scattering data for GyrB consistently yields a “tadpole”-like envelope. It allows us to propose an organization of GyrB into three domains—ATPase, Toprim, and Tail—based on their crystallographic and modeled structures. Our study reveals the modular organization of GyrB and points out its potential flexibility, needed during the gyrase catalytic cycle. It provides important insights into the supercoiling mechanism by gyrase and suggests new lines of research." @default.
- W2068788706 created "2016-06-24" @default.
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- W2068788706 date "2007-03-01" @default.
- W2068788706 modified "2023-09-25" @default.
- W2068788706 title "Modular Structure of the Full-Length DNA Gyrase B Subunit Revealed by Small-Angle X-Ray Scattering" @default.
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- W2068788706 doi "https://doi.org/10.1016/j.str.2007.01.013" @default.
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