Literature citation
Your basket is currently empty.
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
Structure of alpha-latrotoxin oligomers reveals that divalent cation-dependent tetramers form membrane pores.
Orlova E.V., Rahman M.A., Gowen B., Volynski K.E., Ashton A.C., Manser C., van Heel M., Ushkaryov Y.A.
We report here the first three-dimensional structure of alpha-latrotoxin, a black widow spider neurotoxin, which forms membrane pores and stimulates secretion in the presence of divalent cations. We discovered that alpha-latrotoxin exists in two oligomeric forms: it is dimeric in EDTA but forms tetramers in the presence of Ca2+ or Mg2+. The dimer and tetramer structures were determined independently at 18 A and 14 A resolution, respectively, using cryo-electron microscopy and angular reconstitution. The alpha-latrotoxin monomer consists of three domains. The N- and C-terminal domains have been identified using antibodies and atomic fitting. The C4-symmetric tetramers represent the active form of alpha-latrotoxin; they have an axial channel and can insert into lipid bilayers with their hydrophobic base, providing the first model of alpha-latrotoxin pore formation.