› 2ahq

Solution NMR

Solution Structure of the C-terminal RpoN Domain of Sigma-54 from Aquifex aeolicus

Released:
DOI: 10.2210/pdb2ahq/pdb
PDB entry 2ahq coloured by chain, ensemble of 20 models, front view.
PDB entry 2ahq coloured by chain, ensemble of 20 models, side view.
PDB entry 2ahq coloured by chain, ensemble of 20 models, top view.
Source organism: Aquifex aeolicus
Primary publication:
The C-terminal RpoN domain of sigma54 forms an unpredicted helix-turn-helix motif similar to domains of sigma70.
Doucleff M, Malak LT, Pelton JG, Wemmer DE
J Biol Chem 280 41530-6 (2005)
PMID: 16210314

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA polymerase sigma factor RpoN Chain: A
Molecule details ›
Chain: A
Length: 76 amino acids
Theoretical weight: 8.97 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66858 (Residues: 323-398; Coverage: 19%)
Gene names: aq_599, rpoN
Sequence domains: Sigma-54, DNA binding domain
Structure domains: Homeodomain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcription.
Bush et al. (2012)
6 more

4 mentions without citation

Structural biology of bacterial RNA polymerase.
Murakami KS. (2015)
3 more