1DL0

SOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1C

Summary for 1DL0

• Entry DOI: 10.2210/pdb1dl0/pdb
• Descriptor: J-ATRACOTOXIN-HV1C (1 entity in total)
• Functional Keywords: neurotoxin, atracotoxin, insecticidal, cystine knot, vicinal disulfide, toxin
• Cellular location: Secreted: P82228
• Total number of polymer chains: 1
• Total formula weight: 3772.32

Authors

Wang, X.H.,King, G.F. (deposition date: 1999-12-08, release date: 2000-09-15, Last modification date: 2024-11-06)

Primary citation

Wang, X.,Connor, M.,Smith, R.,Maciejewski, M.W.,Howden, M.E.,Nicholson, G.M.,Christie, M.J.,King, G.F.
Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge.
Nat.Struct.Biol., 7:505-513, 2000

PubMed Abstract: We have isolated a family of insect-selective neurotoxins from the venom of the Australian funnel-web spider that appear to be good candidates for biopesticide engineering. These peptides, which we have named the Janus-faced atracotoxins (J-ACTXs), each contain 36 or 37 residues, with four disulfide bridges, and they show no homology to any sequences in the protein/DNA databases. The three-dimensional structure of one of these toxins reveals an extremely rare vicinal disulfide bridge that we demonstrate to be critical for insecticidal activity. We propose that J-ACTX comprises an ancestral protein fold that we refer to as the disulfide-directed beta-hairpin.

PubMed: 10881200
DOI: 10.1038/75921

Experimental method

SOLUTION NMR