2bjv
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CRYSTAL STRUCTURE OF PSPF(1-275) R168A MUTANT
OverviewOverview
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.
About this StructureAbout this Structure
2BJV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into the activity of enhancer-binding proteins., Rappas M, Schumacher J, Beuron F, Niwa H, Bordes P, Wigneshweraraj S, Keetch CA, Robinson CV, Buck M, Zhang X, Science. 2005 Mar 25;307(5717):1972-5. PMID:15790859
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- Escherichia coli
- Single protein
- Beuron, F.
- Bordes, P.
- Buck, M.
- Keetch, C A.
- Niwa, H.
- Rappas, M.
- Robinson, C V.
- Schumacher, J.
- Wigneshweraraj, S.
- Zhang, X.
- Aaa
- Atp-binding
- Dna-binding
- Enhancer binding protein
- Gene regulation
- Pspf
- Sigma54 activator
- Transcription activation
- Transcription regulation