Characterization of the Lipid-Binding Site of Equinatoxin II by NMR and Molecular Dynamics Simulation
Daniel K Weber, Shenggen Yao, Nejc Rojko, Gregor Anderluh, Terry P Lybrand, Matthew T Downton, John Wagner, Frances Separovic
Biophysical Journal | CELL PRESS | Published : 2015
Equinatoxin II (EqtII) is a soluble, 20 kDa pore-forming protein toxin isolated from the sea anemone Actinia equina. Although pore formation has long been known to occur in distinct stages, including monomeric attachment to phospholipid membranes followed by detachment of the N-terminal helical domain and oligomerization into the final pore assembly, atomistic-level detail of the protein-lipid interactions underlying these events remains elusive. Using high-resolution solution state NMR of uniformly-(15)N-labeled EqtII at the critical micelle concentration of dodecylphosphocholine, we have mapped the lipid-binding site through chemical shift perturbations. Subsequent docking of an EqtII mono..View full abstract
This work was supported by a University of Melbourne Dyason-Vanderbilt Partnership grant, VLSCI Resource Allocation Scheme and grants from the Slovenian Research Agency. D.W. is a recipient of an Australian Postgraduate Award and a Dowd Foundation Postgraduate Research Scholarship.