Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins

Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins

The two-domain protein RfaH, a paralog of the universally conserved NusG/Spt5 transcription factors, is regulated by autoinhibition coupled to the reversible conformational switch of its 60-residue C-terminal Kyrpides, Ouzounis, Woese (KOW) domain between an α-hairpin and a β-barrel. In contrast, Nu...

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Bibliographic Details
Main Authors: Philipp K Zuber, Tina Daviter, Ramona Heißmann, Ulrike Persau, Kristian Schweimer, Stefan H Knauer
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2022-10-01
Series:eLife
Subjects:
fold-switching
NusG proteins
RfaH
metamorphic proteins
KOW domains
Online Access:https://elifesciences.org/articles/76630

Internet

https://elifesciences.org/articles/76630

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