› 7ng9

Electron Microscopy
3.3Å resolution

Trimeric efflux pump Klebsiella TolC

Released:
DOI: 10.2210/pdb7ng9/pdb
PDB entry 7ng9 coloured by chain, front view.
PDB entry 7ng9 coloured by chain, side view.
PDB entry 7ng9 coloured by chain, top view.
Source organism: Klebsiella quasipneumoniae
Primary publication:
Toxin import through the antibiotic efflux channel TolC.
Housden NG, Webby MN, Lowe ED, El-Baba TJ, Kaminska R, Redfield C, Robinson CV, Kleanthous C
OpenAccess logo Nat Commun 12 4625 (2021)
PMID: 34330923
Related structures: EMD-12310

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane protein tolC Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 494 amino acids
Theoretical weight: 54.06 KDa
Source organism: Klebsiella quasipneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1C3Q001 (Residues: 1-486; Coverage: 100%)
Gene names: CP911_05930, H8L09_13410, VKR_00671, tolC
Sequence domains: Outer membrane efflux protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-12310
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Mass spectrometry of intact membrane proteins: shifting towards a more native-like context.
Oluwole et al. (2023)
2 more

3 mentions without citation

Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.
Mayse et al. (2023)
2 more