2bjv
From Proteopedia
CRYSTAL STRUCTURE OF PSPF(1-275) R168A MUTANT
Overview
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 Structure
2BJV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 20:23:16 2008
Categories: 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,transcription activation | Atp-binding | Dna-binding | Enhancer binding protein | Gene regulation | Pspf | Sigma54 activator | Transcription regulation
