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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

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EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding.

Aviv Meir¹, Ahmad Abdelhai¹, Yoni Moskovitz¹

¹Department of Chemistry, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.

Biophysical Journal

|June 22, 2017

Summary

The CusCFBA system in E. coli uses the CusB protein to transport toxic copper and silver ions. Copper binding causes CusB to change shape, likely activating the ion efflux channel.

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Area of Science:

Microbiology
Structural Biology
Biochemistry

Background:

Bacterial cells possess intricate mechanisms to mitigate metal ion toxicity.
The Escherichia coli CusCFBA system is a periplasmic efflux pump crucial for exporting copper (Cu(I)) and silver (Ag(I)) ions.
This system comprises four proteins: CusA, CusB, CusC, and CusF, forming the CusCBA transporter with metallochaperone CusF.

Purpose of the Study:

To investigate the role of the adaptor protein CusB in the CusCFBA efflux system.
To elucidate the conformational changes in CusB upon binding Cu(I) using EPR spectroscopy.
To understand how these changes facilitate metal ion transfer and efflux.

Main Methods:

Electron Paramagnetic Resonance (EPR) spectroscopy was employed to study the full CusB protein.
Conformational dynamics of CusB were analyzed in solution upon coordination with Cu(I) ions.

Main Results:

CusB exists as a dimer in solution.
Cu(I) coordination induces a change in the relative orientation of CusB monomers.
This coordination results in a more compact structure of the CusB dimer.

Conclusions:

Cu(I) binding acts as a switch, altering CusB conformation.
The observed structural and topological changes in CusB are likely critical for activating the ion transport channel.
This mechanism facilitates the transfer of metal ions from CusB to CusC for subsequent efflux from the cell.