› 2m1n

Solution NMR

Solution structure of a chaperone in type III secretion system

Released:
DOI: 10.2210/pdb2m1n/pdb
PDB entry 2m1n coloured by chain, ensemble of 20 models, front view.
PDB entry 2m1n coloured by chain, ensemble of 20 models, side view.
PDB entry 2m1n coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli 3003
Primary publication:
Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion.
Chen L, Ai X, Portaliou AG, Minetti CA, Remeta DP, Economou A, Kalodimos CG
Cell Rep 3 709-15 (2013)
PMID: 23523349

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162950 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type III secretion system filament chaperone CesA Chains: A, B
Molecule details ›
Chains: A, B
Length: 107 amino acids
Theoretical weight: 12.26 KDa
Source organism: Escherichia coli 3003
Expression system: Escherichia coli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 13%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Assembly, structure, function and regulation of type III secretion systems.
Deng et al. (2017)
6 more

1 mention without citation

Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.
Hotinger et al. (2021)