2IAH

Crystal structure of the ferripyoverdine receptor of the outer membrane of Pseudomonas aeruginosa bound to ferripyoverdine.

Summary for 2IAH

• Entry DOI: 10.2210/pdb2iah/pdb
• Related: 1XKH 1XKW
• Related PRD ID: PRD_000723
• Descriptor: Ferripyoverdine receptor, Pyoverdin C-E, SULFATE ION, ... (5 entities in total)
• Functional Keywords: pyoverdine, fpva, tonb box, siderophore, cell membrane, ion transport, tonb dependent receptor, membrane protein
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 2
• Total formula weight: 88081.40

Authors

Wirth, C.,Pattus, F.,Cobessi, D. (deposition date: 2006-09-08, release date: 2007-09-11, Last modification date: 2023-11-15)

Primary citation

Wirth, C.,Meyer-Klaucke, W.,Pattus, F.,Cobessi, D.
From the periplasmic signaling domain to the extracellular face of an outer membrane signal transducer of Pseudomonas aeruginosa: crystal structure of the ferric pyoverdine outer membrane receptor.
J.Mol.Biol., 368:398-406, 2007

PubMed Abstract: The pyoverdine outer membrane receptor, FpvA, from Pseudomonas aeruginosa translocates ferric pyoverdine across the outer membrane through an energy consuming mechanism using the proton motive force and the TonB-ExbB-ExbD energy transducing complex from the inner membrane. We solved the crystal structure of the full-length FpvA bound to iron-pyoverdine at 2.7 A resolution. Signal transduction to an anti-sigma protein of the inner membrane and to TonB-ExbB-ExbD involves the periplasmic domain, which displays a beta-alpha-beta fold composed of two alpha-helices sandwiched by two beta-sheets. One iron-pyoverdine conformer is bound at the extracellular face of FpvA, revealing the conformer selectivity of the binding site. The loop that contains the TonB box, involved in interactions with TonB, and connects the signaling domain to the plug domain of FpvA is not defined in the electron density following the binding of ferric pyoverdine. The high flexibility of this loop is probably necessary for signal transduction through the outer membrane.

PubMed: 17349657
DOI: 10.1016/j.jmb.2007.02.023

Experimental method

X-RAY DIFFRACTION (2.73 Å)