1XKW

Pyochelin outer membrane receptor FptA from Pseudomonas aeruginosa

Summary for 1XKW

• Entry DOI: 10.2210/pdb1xkw/pdb
• Descriptor: Fe(III)-pyochelin receptor, SULFATE ION, LAURYL DIMETHYLAMINE-N-OXIDE, ... (6 entities in total)
• Functional Keywords: tonb dependent receptor, membrane protein
• Biological source: Pseudomonas aeruginosa
• Cellular location: Cell outer membrane: P42512
• Total number of polymer chains: 1
• Total formula weight: 76226.44

Authors

Cobessi, D.,Celia, H.,Pattus, F. (deposition date: 2004-09-30, release date: 2005-10-04, Last modification date: 2023-08-23)

Primary citation

Cobessi, D.,Celia, H.,Pattus, F.
Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa
J.Mol.Biol., 352:893-904, 2005

PubMed Abstract: Pyochelin is a siderophore and virulence factor common to Burkholderia cepacia and several Pseudomonas strains. We describe at 2.0 A resolution the crystal structure of the pyochelin outer membrane receptor FptA bound to the iron-pyochelin isolated from Pseudomonas aeruginosa. One pyochelin molecule bound to iron is found in the protein structure, providing the first three-dimensional structure at the atomic level of this siderophore. The pyochelin molecule provides a tetra-dentate coordination of iron, while the remaining bi-dentate coordination is ensured by another molecule not specifically recognized by the protein. The overall structure of the pyochelin receptor is typical of the TonB-dependent transporter superfamily, which uses the proton motive force from the cytoplasmic membrane through the TonB-ExbB-ExbD energy transducing complex to transport ferric ions across the bacterial outer membrane: a transmembrane 22 beta-stranded barrel occluded by a N-terminal domain that contains a mixed four-stranded beta-sheet. The N-terminal TonB box is disordered in two crystal forms, and loop L8 is found to point towards the iron-pyochelin complex, suggesting that the receptor is in a transport-competent conformation.

PubMed: 16139844
DOI: 10.1016/j.jmb.2005.08.004

Experimental method

X-RAY DIFFRACTION (2 Å)