› 1qc7

X-ray diffraction
2.2Å resolution

T. MARITIMA FLIG C-TERMINAL DOMAIN

Released:
DOI: 10.2210/pdb1qc7/pdb
PDB entry 1qc7 coloured by chain, front view.
PDB entry 1qc7 coloured by chain, side view.
PDB entry 1qc7 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor.
Lloyd SA, Whitby FG, Blair DF, Hill CP
Nature 400 472-5 (1999)
PMID: 10440379

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flagellar motor switch protein FliG Chains: A, B
Molecule details ›
Chains: A, B
Length: 101 amino acids
Theoretical weight: 11.53 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WY63 (Residues: 235-335; Coverage: 30%)
Gene names: TM_0220, fliG
Sequence domains: FliG C-terminal domain
Structure domains: Annexin V; domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P212121
Unit cell:
a: 50.68Å b: 62.44Å c: 88.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.304
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Polar flagellar motility of the Vibrionaceae.
McCarter LL. (2001)
11 more

3 mentions without citation

Structural Conservation and Adaptation of the Bacterial Flagella Motor.
Carroll et al. (2020)
2 more