› 1m1h

X-ray diffraction
1.95Å resolution

Crystal structure of Aquifex aeolicus N-utilization substance G (NusG), Space group I222

Released:
DOI: 10.2210/pdb1m1h/pdb
PDB entry 1m1h coloured by chain, front view.
PDB entry 1m1h coloured by chain, side view.
PDB entry 1m1h coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities.
Steiner T, Kaiser JT, Marinkoviç S, Huber R, Wahl MC
EMBO J 21 4641-53 (2002)
PMID: 12198166

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription termination/antitermination protein NusG Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 28.04 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67757 (Residues: 1-248; Coverage: 100%)
Gene names: aq_1931, nusG
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: I222
Unit cell:
a: 81.1Å b: 86.2Å c: 108.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.259
Expression system: Escherichia coli

Quick links

Citations

13 review citations

A nexus for gene expression-molecular mechanisms of Spt5 and NusG in the three domains of life.
Werner F. (2012)
12 more

6 mentions without citation

Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators.
Mooney et al. (2009)
5 more