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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...
| Autores principales: | , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
eLife Sciences Publications, Ltd
2022
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9683785/ https://www.ncbi.nlm.nih.gov/pubmed/36255050 http://dx.doi.org/10.7554/eLife.76630 |