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ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
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Substrate Uptake by TonB-Dependent Outer Membrane Transporters.

Volkmar Braun1

  • 1Max-Planck-Institute of Biology, Tübingen, Germany.

Molecular Microbiology
|December 3, 2024
PubMed
Summary

TonB protein powers active transport across the outer membrane by interacting with TonB-dependent outer membrane transport proteins (TBDTs). This interaction opens pores, enabling nutrient uptake and facilitating the import of various substrates.

Keywords:
TonB proteinenergy deliverytransport

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • TonB is crucial for active transport across the bacterial outer membrane.
  • TonB-dependent outer membrane transport proteins (TBDTs) form pores regulated by plugs.

Purpose of the Study:

  • To review structural changes in TBDTs upon TonB interaction.
  • To elucidate the ExbB-ExbD complex's role in energy transmission to TonB.

Main Methods:

  • Literature review focusing on structural and biochemical studies.
  • Analysis of protein-protein interactions and energy transduction mechanisms.

Main Results:

  • TonB binding to TBDTs causes plug movement, opening the pore for nutrient translocation.
  • The ExbB-ExbD complex transmits proton motive force energy to TonB.
  • TonB facilitates the import of diverse substrates, including toxins.

Conclusions:

  • TonB-dependent transport is a key mechanism for nutrient and toxin uptake in bacteria.
  • Understanding TonB-TBDT interactions provides insights into bacterial outer membrane permeability and transport regulation.