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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| Hlavní autoři: | , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Portfolio
2019-02-01
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| Edice: | Nature Communications |
| On-line přístup: | https://doi.org/10.1038/s41467-019-08567-6 |
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