› 4j9u

X-ray diffraction
3.8Å resolution

Crystal Structure of the TrkH/TrkA potassium transport complex

Released:
DOI: 10.2210/pdb4j9u/pdb
PDB entry 4j9u coloured by chain, front view.
PDB entry 4j9u coloured by chain, side view.
PDB entry 4j9u coloured by chain, top view.
Source organism: Vibrio parahaemolyticus RIMD 2210633
Primary publication:
Gating of the TrkH ion channel by its associated RCK protein TrkA.
Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, Zhou M
Nature 496 317-22 (2013)
PMID: 23598339

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183336 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Trk system potassium uptake protein TrkH Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 485 amino acids
Theoretical weight: 53.1 KDa
Source organism: Vibrio parahaemolyticus RIMD 2210633
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q87TN7 (Residues: 1-485; Coverage: 100%)
Gene names: VP0032, trkH
Sequence domains: Cation transport protein
Trk system potassium uptake protein TrkA Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 458 amino acids
Theoretical weight: 50.19 KDa
Source organism: Vibrio parahaemolyticus RIMD 2210633
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q87KD2 (Residues: 1-458; Coverage: 100%)
Gene name: VP3045
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand TBR 18 x TBR
Ligand K 4 x K
Ligand NAD 4 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 133.725Å b: 146.627Å c: 163.672Å
α: 90° β: 99.32° γ: 90°
R-values:
R R work R free
0.234 0.232 0.28
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.
Deutscher et al. (2014)
13 more

7 mentions without citation

Structure of potassium channels.
Kuang et al. (2015)
6 more