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Escherichia coli SecA shape and dimensions

B Shilton1, D I Svergun, V V Volkov

  • 1Institute of Molecular Biology and Biotechnology and Department of Biology, University of Crete, Iraklio, Greece.

FEBS Letters
|October 22, 1998
PubMed
Summary
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SecA protein is an elongated molecule in solution. Nucleotide binding does not significantly change its overall shape, indicating localized conformational flexibility crucial for SecA/SecYEG interactions.

Area of Science:

  • Structural Biology
  • Molecular Biophysics
  • Protein Conformation

Background:

  • SecA is a key motor protein involved in protein translocation across membranes.
  • Understanding SecA's conformational flexibility is essential for elucidating its function.
  • Previous studies suggested nucleotide-dependent conformational changes in SecA.

Purpose of the Study:

  • To investigate the overall shape and conformational flexibility of dimeric SecA in solution.
  • To determine the impact of nucleotide binding on SecA's structure.
  • To assess conformational changes in a catalytically active SecA mutant.

Main Methods:

  • Small-angle X-ray scattering (SAXS) was employed to study SecA in solution.
  • Analysis focused on the radius of gyration and molecular shape.

Related Experiment Videos

  • SAXS was performed on wild-type SecA with and without nucleotide analogs and on a hydrolysis-proficient mutant.

    • Main Results:

    • Dimeric SecA exists as a highly elongated molecule (15 nm x 8 nm) in solution.
    • Nucleotide binding (ATP, ADP, AMP-PNP) did not alter the overall radius of gyration of SecA.
    • A SecA mutant capable of multiple ATP hydrolysis cycles showed no SAXS-detectable conformational changes.

    Conclusions:

    • Biochemically observed nucleotide-induced conformational changes in SecA are small-scale and localized.
    • The overall elongated structure of SecA remains largely invariant upon nucleotide interaction.
    • These findings have implications for understanding the mechanism of SecA/SecYEG interaction during protein translocation.