› 3hjl

X-ray diffraction
2.4Å resolution

The structure of full-length FliG from Aquifex aeolicus

Released:
DOI: 10.2210/pdb3hjl/pdb
PDB entry 3hjl coloured by chain, front view.
PDB entry 3hjl coloured by chain, side view.
PDB entry 3hjl coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching.
Lee LK, Ginsburg MA, Crovace C, Donohoe M, Stock D
Nature 466 996-1000 (2010)
PMID: 20676082

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130393 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flagellar motor switch protein FliG Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 37.14 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66891 (Residues: 1-328; Coverage: 100%)
Gene names: aq_653, fliG
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 59.997Å b: 65.84Å c: 67.791Å
α: 90° β: 110.99° γ: 90°
R-values:
R R work R free
0.219 0.216 0.27
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Signal processing in complex chemotaxis pathways.
Porter et al. (2011)
11 more

26 mentions without citation

Molecular architecture of the bacterial flagellar motor in cells.
Zhao et al. (2014)
25 more