1B7D

NEUROTOXIN (TS1) FROM BRAZILIAN SCORPION TITYUS SERRULATUS

Summary for 1B7D

• Entry DOI: 10.2210/pdb1b7d/pdb
• Descriptor: PROTEIN (NEUROTOXIN TS1), PHOSPHATE ION (3 entities in total)
• Functional Keywords: long-chain neurotoxin, toxin
• Biological source: Tityus serrulatus (Brazilian scorpion)
• Total number of polymer chains: 1
• Total formula weight: 6995.98

Authors

Polikarpov, I.,Sanches Jr., M.S.,Marangoni, S.,Toyama, M.H.,Teplyakov, A. (deposition date: 1999-01-21, release date: 1999-07-22, Last modification date: 2024-11-06)

Primary citation

Polikarpov, I.,Junior, M.S.,Marangoni, S.,Toyama, M.H.,Teplyakov, A.
Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins.
J.Mol.Biol., 290:175-184, 1999

PubMed Abstract: The crystal structure of neurotoxin Ts1, a major component of the venom of the Brazilian scorpion Tityus serrulatus, has been determined at 1.7 A resolution. It is the first X-ray structure of a highly toxic anti-mammalian beta-toxin. The folding of the polypeptide chain of Ts1 is similar to that of other scorpion toxins. A cysteine-stabilised alpha-helix/beta-sheet motif forms the core of the flattened molecule. All residues identified as functionally important by chemical modification and site-directed mutagenesis are located on one side of the molecule, which is therefore considered as the Na+channel recognition site. The distribution of charged and non-polar residues over this surface determines the specificity of the toxin-channel interaction. Comparison to other scorpion toxins shows that positively charged groups at positions 1 and 12 as well as a negative charge at position 2 are likely determinants of the specificity of beta-toxins. In contrast, the contribution of the conserved aromatic cluster to the interaction might be relatively small. Comparison of Ts1 to weak beta-toxins from Centruroides sculpturatus Ewing reveals that a number of basic amino acid residues located on the face of the molecule opposite to the binding surface may account for the high toxicity of Ts1.

PubMed: 10388565
DOI: 10.1006/jmbi.1999.2868

Experimental method

X-RAY DIFFRACTION (1.73 Å)