|Entry||Database: PDB / ID: 2ahq|
|Title||Solution Structure of the C-terminal RpoN Domain of Sigma-54 from Aquifex aeolicus|
|Components||RNA polymerase sigma factor RpoN|
|Keywords||TRANSCRIPTION / Sigma-54 / sigma factors / solution structure / RNA polymerase|
|Function / homology|
Function and homology information
DNA-binding transcription activator activity / sigma factor activity / DNA-templated transcription, initiation / DNA binding
RNA polymerase sigma factor 54 / RNA polymerase sigma factor 54, core-binding domain / RNA polymerase sigma factor 54, DNA-binding / RNA polymerase sigma-54 factor, core-binding domain superfamily / Sigma-54 factor, Activator interacting domain (AID) / Sigma-54, DNA binding domain / Sigma-54 factor, core binding domain / Sigma-54 factors family signature 2.
RNA polymerase sigma factor RpoN
|Biological species||Aquifex aeolicus (bacteria)|
|Method||SOLUTION NMR / torsion angle dynamics|
|Authors||Doucleff, M. / Malak, L.T. / Pelton, J.G. / Wemmer, D.E.|
|Citation||Journal: J.Biol.Chem. / Year: 2005|
Title: The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70.
Authors: Doucleff, M. / Malak, L.T. / Pelton, J.G. / Wemmer, D.E.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: RNA polymerase sigma factor RpoN
|#1: Protein/peptide|| |
Mass: 8966.376 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aquifex aeolicus (bacteria) / Gene: rpoN / Plasmid: pet21a / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta (BL21 (DE3) with pLysS) / References: UniProt: O66858
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: Other experiments performed and used for chemical shift assignments and obtaining restraints: CBCA(CO)NH, DQF-COSY, CC(CO)NH, H/D Exchange via N15-HSQC, HNHA - J couplings|
|Sample conditions||Ionic strength: 50 mM Hepes; 250 mM NaCl / pH: 6.8 / Pressure: ambient / Temperature: 298 K|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|NMR spectrometer||Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz|
|Refinement||Method: torsion angle dynamics / Software ordinal: 1 |
Details: Structures are based on a total 1064 restraints: 956 distance and 108 dihedral angle
|NMR representative||Selection criteria: lowest dyana target function|
|NMR ensemble||Conformer selection criteria: target function / Conformers calculated total number: 150 / Conformers submitted total number: 20|
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