› 8ftw

Solution NMR

FliT-FliJ fusion complex

Released:
DOI: 10.2210/pdb8ftw/pdb
PDB entry 8ftw coloured by chain, ensemble of 20 models, front view.
PDB entry 8ftw coloured by chain, ensemble of 20 models, side view.
PDB entry 8ftw coloured by chain, ensemble of 20 models, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Primary publication:
Chaperone Recycling in Late-Stage Flagellar Assembly.
Rossi P, Xing Q, Bini E, Portaliou AG, Clay MC, Warren EM, Khanra NK, Economou A, Kalodimos CG
J Mol Biol 167954 (2023)
PMID: 37330284

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-235766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flagellar FliJ protein; Flagellar protein FliT Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.83 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A1N2 (Residues: 1-95; Coverage: 78%)
  • Canonical: P0A1K1 (Residues: 51-101; Coverage: 35%)
Gene names: STM1962, STM1973, flaO, flaS, fliJ, fliT
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 52%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone.
Dhindwal et al. (2024)
1 more