Download MendeleyStructural Insights Into the Activity of Enhancer-Binding Proteins
Rappas, M., Schumacher, J., Beuron, F., Niwa, H., Bordes, P., Wigneshweraraj, S., Keetch, C.A., Robinson, C.V., Buck, M., Zhang, X.(2005) Science 307: 1972
- PubMed: 15790859
- DOI: https://doi.org/10.1126/science.1105932
- Primary Citation of Related Structures:
2BJV, 2BJW - PubMed Abstract:
Activators of bacterial sigma54-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 F [PspF(1-275)], which is bound to an ATP transition state analog in complex with its basal factor, sigma54. By fitting the crystal structure of PspF(1-275) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma54. 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 sigma54.
Organizational Affiliation:
Department of Biological Sciences, Imperial College London, London, SW7 2AZ, UK.
