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Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP–aluminum fluoride: insights into activator mechanochemical action
Conformational changes in sigma 54 (ς(54)) and ς(54)-holoenzyme depend on nucleotide hydrolysis by an activator. We now show that ς(54) and its holoenzyme bind to the central ATP-hydrolyzing domains of the transcriptional activators PspF and NifA in the presence of ADP–aluminum fluoride, an analog o...
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| Autors principals: | , , , , , , , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Cold Spring Harbor Laboratory Press
2001
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC312774/ https://ncbi.nlm.nih.gov/pubmed/11544185 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.205501 |
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