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ABC Transporters: Importer

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The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
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Methanobactin transport machinery.

Laura M K Dassama1, Grace E Kenney1, Soo Y Ro1

  • 1Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208.

Proceedings of the National Academy of Sciences of the United States of America
|November 4, 2016
PubMed
Summary

Methanotrophic bacteria utilize methanobactin (Mbn) to transport copper (Cu) for particulate methane monooxygenase (pMMO). This study identifies MbnT and MbnE as key proteins involved in the recognition and uptake of Cu-loaded Mbn.

Keywords:
chalkophorecopper transportmetal homeostasismethane monooxygenasemethanobactin

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Area of Science:

  • Microbiology
  • Biochemistry
  • Environmental Science

Background:

  • Methanotrophic bacteria are crucial for methane metabolism, a potent greenhouse gas.
  • Particulate methane monooxygenase (pMMO), a copper-dependent enzyme, catalyzes the initial oxidation of methane.
  • Methanotrophs require copper (Cu) for pMMO activity, which they acquire using a natural product called methanobactin (Mbn).

Purpose of the Study:

  • To investigate the roles of MbnT and MbnE in the cellular uptake of copper-loaded methanobactin (CuMbn).
  • To elucidate the molecular mechanisms underlying CuMbn recognition and transport in methanotrophic bacteria.

Main Methods:

  • Bioinformatic analysis and gene regulation studies.
  • Genetic disruption of the MbnT gene and expression in Escherichia coli.
  • Biophysical studies including interaction analysis and crystal structure determination of MbnE.

Main Results:

  • Disruption of the MbnT gene abolished CuMbn uptake, confirming its role in transport.
  • MbnT expression in E. coli conferred CuMbn uptake ability.
  • MbnT and MbnE showed specific interactions with CuMbn, with MbnE's structure supporting its periplasmic transporter role.
  • MbnT and MbnE exhibited differential selectivity for cognate versus noncognate CuMbns.

Conclusions:

  • MbnT and MbnE are essential proteins for the recognition and active transport of CuMbn in methanotrophs.
  • These findings provide molecular insights into the copper acquisition mechanism essential for methane oxidation.
  • The study highlights specific protein-CuMbn interactions guiding the transport process.