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Erabutoxin b. Initial protein refinement and sequence analysis at 0.140-nm resolution
European Journal of Biochemistry
|December 16, 1985
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.
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:
- 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.
