› 1xkh

X-ray diffraction
3.6Å resolution

Pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa PAO1 bound to pyoverdine

Released:
DOI: 10.2210/pdb1xkh/pdb
PDB entry 1xkh coloured by chain, front view.
PDB entry 1xkh coloured by chain, side view.
PDB entry 1xkh coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution.
Cobessi D, Celia H, Folschweiller N, Schalk IJ, Abdallah MA, Pattus F
J Mol Biol 347 121-34 (2005)
PMID: 15733922

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155774 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ferripyoverdine receptor Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 687 amino acids
Theoretical weight: 78.02 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Pseudomonas aeruginosa
UniProt:
  • Canonical: P48632 (Residues: 129-815; Coverage: 89%)
Gene names: PA2398, fpvA
Sequence domains:
Structure domains:
Pyoverdin C-E Chains: I, J, K
Molecule details ›
Chains: I, J, K
Length: 8 amino acids
Theoretical weight: 997 Da
Source organism: Pseudomonas aeruginosa
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand PVE 3 x PVE
3 modified residues:
Ligand MSE 36 x MSE
Ligand DSN 6 x DSN
Ligand FHO 6 x FHO

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C2
Unit cell:
a: 137.451Å b: 231.342Å c: 121.695Å
α: 90° β: 104.57° γ: 90°
R-values:
R R work R free
0.259 0.259 0.288
Expression systems:
  • Pseudomonas aeruginosa
  • Not provided

Quick links

Citations

26 review citations

Siderophore-based iron acquisition and pathogen control.
Miethke et al. (2007)
25 more

10 mentions without citation

TonB-dependent transporters: regulation, structure, and function.
Noinaj et al. (2010)
9 more