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Related Experiment Videos

Ubiquitous soluble Mg(2+)-ATPase complex. A structural study.

J M Peters1, J R Harris, A Lustig

  • 1Institute of Cell and Tumor Biology, German Cancer Research Center, Heidelberg.

Journal of Molecular Biology
|January 20, 1992
PubMed
Summary

Structural analysis of Xenopus laevis Mg(2+)-ATPase reveals oligomerization is essential for its activity. This abundant nuclear and cytoplasmic protein complex comprises six subunits, forming a hexagonal structure crucial for its function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Mg(2+)-ATPase complexes are vital homo-oligomeric proteins found in the nucleus and cytoplasm.
  • These complexes belong to a novel multigene family of putative Mg(2+)-ATPases.
  • Understanding their structure is key to elucidating their diverse cellular functions.

Purpose of the Study:

  • To perform a detailed structural analysis of the soluble Mg(2+)-ATPase complex from Xenopus laevis.
  • To investigate the role of oligomerization in Mg(2+)-ATPase activity.
  • To propose a molecular model for the Mg(2+)-ATPase complex.

Main Methods:

  • Purification of the soluble Mg(2+)-ATPase complex.
  • Non-denaturing polyacrylamide gel electrophoresis with enzyme activity staining.

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  • Analytical ultracentrifugation and scanning transmission electron microscopy for mass determination.
  • Conventional electron microscopy of negatively stained specimens.
  • Production of 2D crystals for high-resolution structural analysis.

    • Main Results:

    • Mg(2+)-ATPase activity is dependent on protein oligomerization; activity is lost upon subunit dissociation.
    • The native complex has a sedimentation coefficient of 15.3 S and a molecular mass of approximately 612,000 Da, composed of six 97,000 Da subunits.
    • Electron microscopy revealed a hexagonal structure (12 nm diameter, 9 nm height) and dimerized complexes (12 nm diameter, 18.5 nm height).
    • 2D crystals of dimerized complexes yielded hexagonal and longitudinal arrays, enabling low-resolution molecular modeling.

    Conclusions:

    • Oligomerization is an inherent structural principle for the Mg(2+)-ATPase multigene family.
    • This family includes functionally diverse proteins like vesicle fusion and peroxisome assembly proteins.
    • The findings provide insights into the structural organization of this novel ATPase family.