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Structural organization of flagellin.

F Vonderviszt1, H Uedaira, S Kidokoro

  • 1ERATO, Molecular Dynamic Assembly Project, Tsukuba, Japan.

Journal of Molecular Biology
|July 5, 1990
PubMed
Summary
This summary is machine-generated.

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Salmonella typhimurium flagellin has three distinct domains. The central domains (G1, G2) are beta-rich, while the third (G3) and terminal regions exhibit alpha-helical structures, revealing flagellin

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Flagellin, the main component of bacterial flagella, exhibits disordered terminal regions and a structured central core in solution.
  • Understanding flagellin's domain organization and secondary structure is crucial for elucidating its assembly and function.

Purpose of the Study:

  • To investigate the conformational properties and domain organization of Salmonella typhimurium flagellin.
  • To characterize the secondary structure of flagellin and its proteolytic fragments.

Main Methods:

  • Differential scanning calorimetry (DSC) to analyze thermal stability and domain cooperativity.
  • Deconvolution analysis of calorimetric melting profiles.
  • Far-ultraviolet circular dichroism (UV-CD) spectroscopy for secondary structure determination.

Related Experiment Videos

  • Secondary structure prediction algorithms.

    • Main Results:

    • Flagellin comprises three co-operative structural domains (G1, G2, G3).
    • Domains G1 and G2 (residues 179-418) are primarily beta-sheet structures with minimal alpha-helix.
    • Domain G3 is discontinuous (residues 67-178 and 419-448) and contains a mix of alpha-helix and beta-sheet.
    • The terminal regions of flagellin are predominantly alpha-helical.

    Conclusions:

    • Salmonella typhimurium flagellin possesses a defined domain organization with distinct structural characteristics.
    • The central region is rich in beta-structure, contributing to protease resistance, while terminal regions are alpha-helical.
    • This domain composition likely influences flagellin polymerization and filament formation.