› 2k06

Solution NMR

Solution structure of the aminoterminal domain of E. coli NusG

Released:
DOI: 10.2210/pdb2k06/pdb
PDB entry 2k06 coloured by chain, ensemble of 20 models, front view.
PDB entry 2k06 coloured by chain, ensemble of 20 models, side view.
PDB entry 2k06 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators.
Mooney RA, Schweimer K, Rösch P, Gottesman M, Landick R
J Mol Biol 391 341-58 (2009)
PMID: 19500594

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription termination/antitermination protein NusG Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 14.1 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AFG0 (Residues: 1-123; Coverage: 68%)
Gene names: JW3945, b3982, nusG
Sequence domains: Transcription termination factor nusG
Structure domains: NusG, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

29 review citations

Evolution of multisubunit RNA polymerases in the three domains of life.
Werner et al. (2011)
28 more

21 mentions without citation

Ubiquitous transcription factors display structural plasticity and diverse functions: NusG proteins - Shifting shapes and paradigms.
NandyMazumdar et al. (2015)
20 more