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Related Experiment Videos

Erabutoxin b. Initial protein refinement and sequence analysis at 0.140-nm resolution.

P E Bourne, A Sato, P W Corfield

    European Journal of Biochemistry
    |December 16, 1985
    PubMed
    Summary

    Structural refinement of erabutoxin b revealed two sequence errors, correcting previous conflicts with experimental data. This neurotoxin shares structural identity with related toxins from sea-snake venom.

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    Neuroscience research·1992

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Neuroscience

    Background:

    • Erabutoxin b is a postsynaptic neurotoxin found in sea-snake venom.
    • Previous structural and chemical data for erabutoxin b had inconsistencies.

    Purpose of the Study:

    • To refine the crystal structure of erabutoxin b.
    • To resolve discrepancies between structural and experimental data.
    • To confirm structural identity with other sea-snake venom toxins.

    Main Methods:

    • Restrained least-squares refinement of crystal structure.
    • Interactive computer graphics for structural analysis.
    • Chemical analysis for sequence confirmation.

    Main Results:

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  • The crystal structure of erabutoxin b was refined to 0.140-nm resolution.
  • Two chemical sequence errors (His6-Gln7 and Ser18-Pro19) were identified and corrected.
  • The refined structure confirmed the discontinuous nature of a beta sheet.
  • Structural identity was established between erabutoxin b and neurotoxin b from different geographical sources.

    • Conclusions:

    • Corrected erabutoxin b sequence resolves previous experimental conflicts.
    • The refined structure provides a more accurate model for erabutoxin b.
    • Structural identity of toxins from different sea-snake populations was confirmed.