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The structural basis for regulated assem ... transcriptional activator NtrC
The structural basis for regulated assembly and function of the transcriptional activator NtrC
7335
In two-component signal transduction, an input triggers phosphorylation of receiver domains that regulate the status of output modules. One such module is the AAA+ ATPase domain in bacterial enhancer-binding proteins that remodel the sigma(54) form of RNA polymerase. We report X-ray solution scattering and electron microscopy structures of the activated, full-length nitrogen-regulatory protein C (NtrC) showing a novel mechanism for regulation of AAA+ ATPase assembly via the juxtaposition of the receiver domains and ATPase ring. Accompanying the hydrolysis cycle that is required for transcriptional activation, we observed major order-disorder changes in the GAFTGA loops involved in sigma(54) binding, as well as in the DNA-binding domains.
De Carlo S, Chen B, Hoover TR, Kondrashkina E, Nogales E, Nixon BT
Genes & development
2006-06-01 00:00
20
11
1485-95
Escherichia coli Proteins,Hydrolysis,Microscopy, Electron,PII Nitrogen Regulatory Proteins,Phosphorylation,Scattering, Radiation,Trans-Activators,Transcription Factors,Escherichia coli Proteins,PII Nitrogen Regulatory Proteins,Trans-Activators,Transcription Factors,glnG protein, E coli
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA.
Genes Dev.
NCRR RR-08630
0890-9369
10.1101/gad.1418306
20/11/1485
0
False
16751184
