https://ns11394modulator.com/a....ssociation-involving
Here, we report the single-particle cryo-electron microscopy structures of T. thermophilus Mfd-RNAP complex with and without ATPγS. The structures reveal that Mfd undergoes serious conformational modifications upon activation, contacts the RNAP β1 domain and its own clamp, and pries start the RNAP clamp. These structures supply a foundation for future studies aimed at dissecting the particular system of Mfd-dependent transcription termination and pave just how for log
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