1XKH

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

1XKH の概要

• エントリーDOI: 10.2210/pdb1xkh/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000507
• 分子名称: Ferripyoverdine receptor, Pyoverdin C-E, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: pyoverdine, fpva, tonb box, siderophore, cell membrane, ion transport, tonb dependent receptor, membrane protein
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• 細胞内の位置: Cell outer membrane: P48632
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 238455.67

構造登録者

Cobessi, D.,Celia, H.,Folschweiller, N.,Schalk, I.J.,Abdallah, M.A.,Pattus, F. (登録日: 2004-09-29, 公開日: 2005-03-15, 最終更新日: 2024-04-03)

主引用文献

Cobessi, D.,Celia, H.,Folschweiller, N.,Schalk, I.J.,Abdallah, M.A.,Pattus, F.
The Crystal Structure of the Pyoverdine Outer Membrane Receptor FpvA from Pseudomonas aeruginosa at 3.6A Resolution
J.Mol.Biol., 347:121-134, 2005

PubMed Abstract: The pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa translocates ferric-pyoverdine across the outer membrane via an energy consuming mechanism that involves the inner membrane energy transducing complex of TonB-ExbB-ExbD and the proton motive force. We solved the crystal structure of FpvA loaded with iron-free pyoverdine at 3.6 angstroms resolution. The pyoverdine receptor is folded in two domains: a transmembrane 22-stranded beta-barrel domain occluded by an N-terminal domain containing a mixed four-stranded beta-sheet (the plug). The beta-strands of the barrel are connected by long extracellular loops and short periplasmic turns. The iron-free pyoverdine is bound at the surface of the receptor in a pocket lined with aromatic residues while the extracellular loops do not completely cover the pyoverdine binding site. The TonB box, which is involved in intermolecular contacts with the TonB protein of the inner membrane, is observed in an extended conformation. Comparison of this first reported structure of an iron-siderophore transporter from a bacterium other than Escherichia coli with the known structures of the E.coli TonB-dependent transporters reveals a high structural homology and suggests that a common sensing mechanism exists for the iron-loading status in all bacterial iron siderophore transporters.

PubMed: 15733922
DOI: 10.1016/j.jmb.2005.01.021

実験手法

X-RAY DIFFRACTION (3.6 Å)