PMID:15790859
| Citation |
Rappas, M, Schumacher, J, Beuron, F, Niwa, H, Bordes, P, Wigneshweraraj, S, Keetch, CA, Robinson, CV, Buck, M and Zhang, X (2005) Structural insights into the activity of enhancer-binding proteins. Science 307:1972-5 |
|---|---|
| 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. |
| Links |
PubMed PMC2756573 Online version:10.1126/science.1105932 |
| Keywords |
Adenosine Triphosphate/metabolism; Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Cryoelectron Microscopy; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; DNA-Directed RNA Polymerases/chemistry; DNA-Directed RNA Polymerases/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrolysis; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Molecular Sequence Data; Mutation; PII Nitrogen Regulatory Proteins; Protein Conformation; Protein Folding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; RNA Polymerase Sigma 54; Sigma Factor/chemistry; Sigma Factor/metabolism; Trans-Activators/chemistry; Trans-Activators/metabolism; Transcription Factors/chemistry; Transcription Factors/metabolism |
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