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Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 Å

Xiuhua Liu1, Qian Du, Zhi Wang

  • 1State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China.

FEBS Letters
|May 12, 2012
PubMed

Insights

Vibrio cholerae

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Vibrio cholerae utilizes siderophore-binding proteins (PBPs) for iron acquisition.
  • VctP is essential for transporting enterobactin and vibriobactin, crucial siderophores with distinct iron coordination.
  • Understanding VctP's structure is key to its function in iron transport.

Purpose of the Study:

  • To determine the crystal structure of VctP from Vibrio cholerae N16961.
  • To elucidate the structural basis for VctP's interaction with enterobactin and vibriobactin.
  • To identify key residues involved in binding these two different siderophores.

Main Methods:

  • X-ray crystallography at 1.7Å resolution.
  • Structural comparison with homologous proteins.
  • Molecular docking simulations.

Main Results:

  • The crystal structure of VctP was determined at 1.7Å resolution.
  • Enterobactin and vibriobactin share a common binding pocket within VctP.
  • A basic triad (Arg137, Arg226, Arg270) binds ferric-enterobactin, while a basic dyad (Arg137, Arg270) binds ferric-vibriobactin.

Conclusions:

  • VctP employs a shared binding pocket for structurally distinct siderophores.
  • Specific arginine residues are critical for coordinating the different charges of ferric-enterobactin and ferric-vibriobactin.
  • This structural insight aids in understanding iron uptake mechanisms in Vibrio cholerae.

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