Reversible fold-switching controls the functional cycle of the antitermination factor RfaH

The antitermination factor RfaH adopts two functional states where its C-terminal domain is folded either as an α-helical hairpin or β-barrel. Here the authors employ solution state NMR measurements to show that the C-terminal domain transforms into the β-barrel only upon binding to the elongation c...

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Bibliographic Details
Main Authors: Philipp Konrad Zuber, Kristian Schweimer, Paul Rösch, Irina Artsimovitch, Stefan H. Knauer
Format: Article
Language:English
Published: Nature Publishing Group 2019-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-08567-6