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Related Experiment Videos

Direct visualisation of conformational changes in EF(0)F(1) by electron microscopy.

B Böttcher1, I Bertsche, R Reuter

  • 1Institut für Physikalische Chemie, Albertstrasse 23a, Universität Freiburg, D-79104, Germany. bottcher@embl-heidelberg.de

Journal of Molecular Biology
|February 12, 2000
PubMed
Summary

The structure of Escherichia coli H(+)-ATPase (EF(0)F(1)) was mapped in 3D. Binding of AMP-PNP induced significant conformational changes in the F(1)-part, altering its shape and internal cavities.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • H(+)-ATPases are crucial proton pumps in cellular energy production.
  • The Escherichia coli H(+)-ATPase (EF(0)F(1)) is a key model for studying these enzymes.

Purpose of the Study:

  • To elucidate the three-dimensional structure of EF(0)F(1) using electron microscopy.
  • To investigate conformational changes in EF(0)F(1) upon substrate analogue binding.

Main Methods:

  • Single-particle image processing of negatively stained EF(0)F(1) molecules.
  • Calculation of three-dimensional maps in the absence and presence of AMP-PNP.

Main Results:

  • 3D maps revealed a prominent stalk connecting F(1) to F(0) and a thinner stator stalk.

Related Experiment Videos

  • AMP-PNP binding caused a decrease in the F(1)-part diameter and formation of a pointed cap.
  • Internal cavities within the F(1)-part showed altered patterns upon AMP-PNP binding.

    • Conclusions:

    • The study provides detailed structural insights into EF(0)F(1) and its conformational flexibility.
    • Substrate analogue binding induces significant structural rearrangements in the F(1)-domain of H(+)-ATPase.