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- W4306698552 abstract "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, NusG/Spt5-KOW domains only occur in the β-barrel state. To understand the principles underlying the drastic fold switch in RfaH, we elucidated the thermodynamic stability and the structural dynamics of two RfaH- and four NusG/Spt5-KOW domains by combining biophysical and structural biology methods. We find that the RfaH-KOW β-barrel is thermodynamically less stable than that of most NusG/Spt5-KOWs and we show that it is in equilibrium with a globally unfolded species, which, strikingly, contains two helical regions that prime the transition toward the α-hairpin. Our results suggest that transiently structured elements in the unfolded conformation might drive the global folding transition in metamorphic proteins in general." @default.
- W4306698552 created "2022-10-19" @default.
- W4306698552 creator A5010484728 @default.
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- W4306698552 date "2022-10-18" @default.
- W4306698552 modified "2023-10-01" @default.
- W4306698552 title "Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins" @default.
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- W4306698552 doi "https://doi.org/10.7554/elife.76630" @default.
- W4306698552 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36255050" @default.
- W4306698552 hasPublicationYear "2022" @default.
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