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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Detalhes bibliográficos
Main Authors: Chaney, Matthew, Grande, Ricardo, Wigneshweraraj, Siva R., Cannon, Wendy, Casaz, Paul, Gallegos, Maria-Trinidad, Schumacher, Jorg, Jones, Susan, Elderkin, Sarah, Dago, Angel Ernesto, Morett, Enrique, Buck, Martin
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 2001
Assuntos:
Research Paper
Acesso em linha: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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