An excitatory scorpion toxin with a distinctive feature: An additional α helix at the C terminus and its implications for interaction with insect sodium channels

Deena A. Oren, Oren Froy, Efrat Amit, Nurit Kleinberger-Doron, Michael Gurevitz, Boaz Shaanan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

68 Scopus citations


Background: Scorpion neurotoxins, which bind and modulate sodium channels, have been divided into two groups, the α and β toxins, according to their activities. The β-toxin class includes the groups of excitatory and depressant toxins, which differ in their mode of action and are highly specific against insects. The three-dimensional structures of several α and β toxins have been determined at high resolution, but no detailed 3D structure of an excitatory toxin has been presented so far. Results: The crystal structure of an anti-insect excitatory toxin from the scorpion Buthotus judaicus, Bj-xtrlT, has been determined at 2.1 Å resolution and refined to an R factor of 0.209. The first 59 residues form a closely packed module, structurally similar to the conserved α and β toxins ('long toxins') affecting sodium channels. The last 17 residues form a C-terminal extension not previously seen in scorpion toxins. It comprises a short α helix anchored to the N-terminal module by a disulfide bridge and is followed by a highly mobile stretch of seven residues, of which only four are seen in the electron-density map. This mobile peptide covers part of a conserved hydrophobic surface that is thought to be essential for interaction with the channel in several long toxins. Conclusions: Replacement of the last seven residues by a single glycine abolishes the activity of Bj-xtrlT, strongly suggesting that these residues are intimately involved in the interaction with the channel. Taken together with the partial shielding of the conserved hydrophobic surface and the proximity of the C terminus to an adjacent surface rich in charged residues, it seems likely that the bioactive surface of Bj-xtrlT is formed by residues surrounding the C terminus. The 3D structure and a recently developed expression system for Bj-xtrlT pave the way for identifying the structural determinants involved in the bioactivity and anti-insect specificity of excitatory toxins.

Original languageAmerican English
Pages (from-to)1095-1103
Number of pages9
Issue number9
StatePublished - 15 Sep 1998
Externally publishedYes

Bibliographical note

Funding Information:
This research was supported by the Da'at Consortium, a Magnet project administered by the office of the Chief Scientist of the Ministry of Industry & Trade, Israel (BS); Grant IS-2486-94C from BARD, the United States–Israel Binational Agricultural Research & Development Fund (MG and BS); Grant 891-0112-95 from the Israeli Ministry of Agriculture (MG) and Grant 466/97 from the Israel Academy of Sciences and Humanities (MG).


  • Crystal structure
  • Excitatory toxin
  • Insecticides
  • Scorpion toxin
  • Sodium channels


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