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TonB-dependent receptors-structural perspectives.

Andrew D Ferguson1, Johann Deisenhofer

  • 1Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9050, USA.

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Iron uptake in bacteria relies on siderophores and TonB-dependent receptors. Structural analysis reveals these outer membrane transporters have a unique beta-barrel and plug domain structure, explaining iron transport mechanisms.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Microorganisms like bacteria, fungi, and yeast use siderophores for iron acquisition, crucial for host interactions and survival.
  • Gram-negative bacteria employ TonB-dependent receptors for transporting siderophores across the outer membrane into the periplasm.
  • The TonB, ExbB, and ExbD protein complex links cytoplasmic membrane energy to outer membrane transport.

Purpose of the Study:

  • To elucidate the structural basis of siderophore transport across the bacterial outer membrane.
  • To understand the mechanism of signal transduction in TonB-dependent receptors.

Main Methods:

  • Crystallographic structure determination of two TonB-dependent receptors (FhuA and FepA).
  • Analysis of the structural components, including the beta-barrel and plug domains.

Main Results:

  • Revealed a novel two-domain structure for TonB-dependent receptors: a 22-stranded antiparallel beta-barrel and an internal plug domain.
  • The beta-barrel forms the outer membrane channel, connected by loops and turns.
  • The plug domain consists of beta-sheets and alpha-helices, positioned within the beta-barrel.

Conclusions:

  • Siderophore binding triggers conformational changes, providing a structural basis for signal transduction.
  • The determined structures suggest a mechanism for siderophore transport across the outer membrane.