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Structure of the P-type ATPases

W Kühlbrandt1, M Auer, G A Scarborough

  • 1Max-Planck-Institut für Biophysik, Abteilung Strukturbiologie, Frankfurt am Main, Germany. kuehlbrandt@biophys.mpg.de

Current Opinion in Structural Biology
|September 8, 1998
PubMed
Summary

Electron cryocrystallography revealed structural differences between the plasma membrane H+-ATPase and Ca2+-ATPase. While their membrane regions are similar, the cytoplasmic domains show significant variations, impacting their function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Research

Background:

  • The neurospora plasma membrane H+-ATPase and sarcoplasmic reticulum Ca2+-ATPase are crucial ion transporters.
  • Understanding their structures is key to elucidating ion transport mechanisms.

Purpose of the Study:

  • To determine and compare the structures of H+-ATPase and Ca2+-ATPase using electron cryocrystallography.
  • To identify structural similarities and differences between these related ion transporters.

Main Methods:

  • Electron cryocrystallography was employed to analyze precipitant-induced two-dimensional surface crystals of H+-ATPase and tubular crystals of Ca2+-ATPase.
  • High-resolution structure maps were generated at approximately 8 Å resolution.

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Main Results:

  • Structure maps revealed comparable membrane-embedded regions for both H+-ATPase and Ca2+-ATPase.
  • Significant structural differences were observed in the cytoplasmic regions of the two enzymes.

Conclusions:

  • Despite close evolutionary relationships, the distinct cytoplasmic domains suggest divergent functional roles or regulatory mechanisms.
  • These findings provide insights into the structural diversity of P-type ATPases.