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A structural framework for unidirectional transport by a bacterial ABC exporter.

Chengcheng Fan1, Jens T Kaiser1, Douglas C Rees2,3

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125.

Proceedings of the National Academy of Sciences of the United States of America
|July 25, 2020
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Summary

This study reveals how Novosphingobium aromaticivorans Atm1 (NaAtm1) exports glutathione, using structural insights from crystallography and cryo-EM. TM6 kinking in NaAtm1 controls substrate binding, ensuring unidirectional transport.

Keywords:
ABC transportersATP-binding cassette transportersalternating access mechanismglutathione transporttransport cycle

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Molecular Transport

Background:

  • The ATP-binding cassette (ABC) transporter of mitochondria (Atm1) is crucial for iron homeostasis in eukaryotes.
  • The prokaryotic homolog, NaAtm1 from Novosphingobium aromaticivorans, exports glutathione and protects against heavy metals.

Purpose of the Study:

  • To elucidate the structural basis of NaAtm1's transport mechanism.
  • To understand how NaAtm1 achieves unidirectional export of glutathione derivatives.

Main Methods:

  • X-ray crystallography and single-particle cryo-electron microscopy were used to determine eight distinct structures of NaAtm1.
  • Disulfide crosslinks and nucleotides stabilized various conformational states of the transporter.

Main Results:

  • Conformational changes in transmembrane helix 6 (TM6) dynamically alter the glutathione-binding site.
  • Kinking of TM6 in the post-ATP hydrolysis state eliminates the binding cavity, preventing substrate uptake.
  • The transient presence and subsequent absence of the binding cavity enforce unidirectional transport.

Conclusions:

  • NaAtm1 utilizes a simple yet elegant mechanism involving TM6 conformational changes to ensure directional export.
  • A functional variant suggests that Atm1 transport may involve limited conformational states with minimal nucleotide-binding domain separation.