› 5wrh

Electron Microscopy
7.4Å resolution

FlgG structure based on the CryoEM map of the bacterial flagellar polyrod

Released:
DOI: 10.2210/pdb5wrh/pdb
PDB entry 5wrh coloured by chain, front view.
PDB entry 5wrh coloured by chain, side view.
PDB entry 5wrh coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Primary publication:
Identical folds used for distinct mechanical functions of the bacterial flagellar rod and hook.
Fujii T, Kato T, Hiraoka KD, Miyata T, Minamino T, Chevance FF, Hughes KT, Namba K
Nat Commun 8 14276 (2017)
PMID: 28120828
Related structures: EMD-6683

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 22-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141006 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flagellar basal-body rod protein FlgG Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 27.78 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
UniProt:
  • Canonical: P0A1J3 (Residues: 1-260; Coverage: 100%)
Gene names: STM1179, fla FVII, flaL, flgG
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 7.4Å
Relevant EMDB volumes: EMD-6683

Quick links

Citations

9 review citations

Dynamic exchange of two types of stator units in Bacillus subtilis flagellar motor in response to environmental changes.
Terahara et al. (2020)
8 more

3 mentions without citation

Identical folds used for distinct mechanical functions of the bacterial flagellar rod and hook.
Fujii et al. (2017)
2 more