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| Title | Three-dimensional EM structure of an intact activator-dependent transcription initiation complex. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 106, Issue 47, Page 19830-19835, Year 2009 |
| Publish date | Nov 24, 2009 |
Authors | Brian P Hudson / Joel Quispe / Samuel Lara-González / Younggyu Kim / Helen M Berman / Eddy Arnold / Richard H Ebright / Catherine L Lawson / ![]() |
| PubMed Abstract | We present the experimentally determined 3D structure of an intact activator-dependent transcription initiation complex comprising the Escherichia coli catabolite activator protein (CAP), RNA ...We present the experimentally determined 3D structure of an intact activator-dependent transcription initiation complex comprising the Escherichia coli catabolite activator protein (CAP), RNA polymerase holoenzyme (RNAP), and a DNA fragment containing positions -78 to +20 of a Class I CAP-dependent promoter with a CAP site at position -61.5 and a premelted transcription bubble. A 20-A electron microscopy reconstruction was obtained by iterative projection-based matching of single particles visualized in carbon-sandwich negative stain and was fitted using atomic coordinate sets for CAP, RNAP, and DNA. The structure defines the organization of a Class I CAP-RNAP-promoter complex and supports previously proposed interactions of CAP with RNAP alpha subunit C-terminal domain (alphaCTD), interactions of alphaCTD with sigma(70) region 4, interactions of CAP and RNAP with promoter DNA, and phased-DNA-bend-dependent partial wrapping of DNA around the complex. The structure also reveals the positions and shapes of species-specific domains within the RNAP beta', beta, and sigma(70) subunits. |
External links | Proc Natl Acad Sci U S A / PubMed:19903881 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 19.8 Å |
| Structure data | |
| Chemicals | ![]() ChemComp-CMP: |
| Source |
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Keywords | TRANSCRIPTION/DNA / transcription / initiation / Class I / activator / RNA polymerase / holoenzyme / sigma70 / open complex / CAP / CRP / cAMP-dependent / DNA / prokaryotic / DNA-directed RNA polymerase / Nucleotidyltransferase / Transferase / DNA-binding / Sigma factor / Transcription regulation / cAMP / cAMP-binding / Nucleotide-binding / TRANSCRIPTION-DNA COMPLEX |
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