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The ArsD As(III) metallochaperone.

A Abdul Ajees¹, Jianbo Yang, Barry P Rosen

¹Department of Cellular Biology and Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, FL 33199, USA.

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine

|December 29, 2010

Summary

Arsenic resistance in E. coli involves the ArsD chaperone transferring toxic arsenic (As(III)) to the ArsA pump. This interaction, crucial for cellular defense, involves specific surface residues on ArsD.

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Area of Science:

Biochemistry
Molecular Biology
Environmental Health

Background:

Arsenic is a toxic metalloid causing health issues.
The ars operon in E. coli plasmid R773 confers arsenic resistance.
ArsA is the catalytic subunit of the As(III) extrusion pump, and ArsD is its arsenic chaperone.

Purpose of the Study:

To investigate the interaction between the ArsD arsenic chaperone and the ArsA ATPase.
To identify the specific binding interface and residues involved in As(III) transfer.
To understand the mechanism of arsenic resistance conferred by the ArsAB pump.

Main Methods:

X-ray crystallography of ArsD at 1.4 Å resolution.
In silico molecular docking of ArsD with ArsA.
Site-directed mutagenesis of ArsD to assess interaction strength with ArsA.

Main Results:

ArsD possesses a thioredoxin fold with a three sulfur-coordinated As(III) binding site (Cys12, Cys13, Cys18).
ArsA's ATP hydrolysis is necessary for As(III) transfer from ArsD.
Mutagenesis studies confirmed that the α1 helix surface and metalloid binding site of ArsD mediate interaction with ArsA.

Conclusions:

The ArsD-ArsA interface involves specific surface residues on ArsD, including the α1 helix.
Understanding this interaction is key to elucidating the mechanism of arsenic detoxification.
This research provides insights into metallochaperone-ATPase interactions for arsenic resistance.