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Title | The structural basis for regulated assembly and function of the transcriptional activator NtrC. |
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Journal, issue, pages | Genes Dev, Vol. 20, Issue 11, Page 1485-1495, Year 2006 |
Publish date | Jun 1, 2006 |
Authors | Sacha De Carlo / Baoyu Chen / Timothy R Hoover / Elena Kondrashkina / Eva Nogales / B Tracy Nixon / |
PubMed Abstract | 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- ...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. |
External links | Genes Dev / PubMed:16751184 / PubMed Central |
Methods | EM (single particle) |
Resolution | 28.0 Å |
Structure data | EMDB-1218: |
Source |
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