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Solution NMR

Solution Structure of the periplasmic domain of TolR from Haemophilus influenzae

Released:
DOI: 10.2210/pdb2jwk/pdb
PDB entry 2jwk coloured by chain, ensemble of 20 models, front view.
PDB entry 2jwk coloured by chain, ensemble of 20 models, side view.
PDB entry 2jwk coloured by chain, ensemble of 20 models, top view.
Source organism: Haemophilus influenzae
Primary publication:
The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data.
Parsons LM, Grishaev A, Bax A
Biochemistry 47 3131-42 (2008)
PMID: 18269247

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tol-Pal system protein TolR Chains: A, B
Molecule details ›
Chains: A, B
Length: 74 amino acids
Theoretical weight: 8.01 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P43769 (Residues: 59-130; Coverage: 52%)
Gene names: HI_0384, tolR
Sequence domains: Biopolymer transport protein ExbD/TolR
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Bacterial outer membrane constriction.
Egan AJF. (2018)
3 more

8 mentions without citation

The multifarious roles of Tol-Pal in Gram-negative bacteria.
Szczepaniak et al. (2020)
7 more