Journal
SCIENCE
Volume 307, Issue 5717, Pages 1972-1975Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1105932
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- Biotechnology and Biological Sciences Research Council [B17129] Funding Source: Medline
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Activators of bacterial sigma(54)-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic electron microscopy (cryo-EM) a 20 angstrom resolution structure of an activator, phage shock protein IF [PspF((1-275))], which is bound to an ATP transition state analog in complex with its basal factor, sigma(54). By fitting the crystal structure of PspF((1-275)) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma(54). Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma(54)..
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