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Related Experiment Videos

Trimeric ring-like structure of ArsA ATPase.

H W Wang1, Y J Lu, L J Li

  • 1State Key Laboratory of Biomembrane & Membrane Biotechnology, Department of Biological Sciences & Biotechnology, Tsinghua University, Beijing, PR China.

FEBS Letters
|March 10, 2000
PubMed
Summary

The ArsA protein, a key component of the Escherichia coli anion pump, functions as an ATPase. Studies reveal that ArsA primarily exists as a trimer when bound to arsenite in solution.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The ArsA protein is the soluble ATPase subunit of the Ars anion pump in Escherichia coli.
  • It hydrolyzes ATP, providing energy for the membrane-bound ArsB subunit to extrude arsenite or antimonite from the cytoplasm.
  • Understanding ArsA's oligomeric state is crucial for elucidating its function in arsenic resistance.

Purpose of the Study:

  • To determine the oligomeric state of the ArsA protein in solution, particularly when bound to its substrate arsenite.
  • To investigate the structural organization of ArsA using biophysical and imaging techniques.

Main Methods:

  • Two-dimensional crystallization of ArsA in the presence of arsenite on a negatively-charged lipid monolayer.
  • Electron microscopy of negatively-stained specimens followed by image processing to obtain a projection map.

Related Experiment Videos

  • Size-exclusion chromatography to determine the molecular weight of ArsA particles in solution.

    • Main Results:

    • A projection map at 2.4 nm resolution revealed a ring-like structure with threefold symmetry for ArsA crystals.
    • Dispersed molecular assemblies with similar ring-like structures were observed in purified ArsA solutions.
    • Size-exclusion chromatography indicated that ArsA particles in solution with arsenite have a molecular weight of approximately 180 kDa.

    Conclusions:

    • The ArsA ATPase, when bound to substrate (arsenite), predominantly exists in a trimeric form in solution.
    • These findings provide insights into the structural basis of ArsA function in arsenic detoxification.
    • The trimeric ring-like structure likely plays a role in the ATP hydrolysis mechanism powering the anion pump.