+Search query
-Structure paper
Title | Structural insights into the activity of enhancer-binding proteins. |
---|---|
Journal, issue, pages | Science, Vol. 307, Issue 5717, Page 1972-1975, Year 2005 |
Publish date | Mar 25, 2005 |
![]() | Mathieu Rappas / Jorg Schumacher / Fabienne Beuron / Hajime Niwa / Patricia Bordes / Sivaramesh Wigneshweraraj / Catherine A Keetch / Carol V Robinson / Martin Buck / Xiaodong Zhang / ![]() |
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 ...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. |
![]() | ![]() ![]() ![]() |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.7 - 20.0 Å |
Structure data | ![]() EMDB-1109: ![]() PDB-2bjv: ![]() PDB-2bjw: |
Chemicals | ![]() ChemComp-HOH: |
Source |
|
![]() | ![]() ![]() ![]() |