Proteopedia

1dl0

SOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1CSOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1C

Structural highlights

1dl0 is a 1 chain structure with sequence from Hadronyche versuta. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TK1C_HADVE This excitatory toxin inhibits insect calcium-activated potassium (KCa) channels (Slo-type). Pan-neuronal expression in Drosophila is lethal but flies engineered to express the toxin only in clock neurons have defects in circadian rhythm but a normal lifespan.[1] [2] [3] [4]

Publication Abstract from PubMed

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.

Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge.,Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF Nat Struct Biol. 2000 Jun;7(6):505-13. PMID:10881200[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF. Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol. 2000 Jun;7(6):505-13. PMID:10881200 doi:http://dx.doi.org/10.1038/75921
  2. ↑ Tedford HW, Maggio F, Reenan RA, King G. A model genetic system for testing the in vivo function of peptide toxins. Peptides. 2007 Jan;28(1):51-6. Epub 2006 Dec 1. PMID:17141372 doi:http://dx.doi.org/10.1016/j.peptides.2006.08.026
  3. ↑ Gunning SJ, Maggio F, Windley MJ, Valenzuela SM, King GF, Nicholson GM. The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels. FEBS J. 2008 Aug;275(16):4045-59. doi: 10.1111/j.1742-4658.2008.06545.x. Epub, 2008 Jul 9. PMID:18625007 doi:http://dx.doi.org/10.1111/j.1742-4658.2008.06545.x
  4. ↑ Wu Y, Cao G, Pavlicek B, Luo X, Nitabach MN. Phase coupling of a circadian neuropeptide with rest/activity rhythms detected using a membrane-tethered spider toxin. PLoS Biol. 2008 Nov 4;6(11):e273. doi: 10.1371/journal.pbio.0060273. PMID:18986214 doi:http://dx.doi.org/10.1371/journal.pbio.0060273
  5. ↑ Wang X, Connor M, Smith R, Maciejewski MW, Howden ME, Nicholson GM, Christie MJ, King GF. Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge. Nat Struct Biol. 2000 Jun;7(6):505-13. PMID:10881200 doi:http://dx.doi.org/10.1038/75921
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