PDB ID or protein name

1iaz » Equinatoxin II

1iaz » Equinatoxin II
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Topology in Secreted
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in side
1iaz » Equinatoxin II
Hydrophobic Thickness 3.0 ± 1.2 Å
Tilt Angle 44 ± 9°
ΔGtransfer -5.1 kcal/mol
Links to 1iaz PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution 1.9 Å
Other PDB entries representing this structure 1kd6, 1tzq
Number of TM subunits 1
Experimental Verification for 1iaz » Equinatoxin II
W112 has been identified as buried in the hydrophobic core of phospholipid micelles or bicelles (Hong et al. 2002, Anderluh et al. 2005), which is consistent with the set of calculated buried residues P81, V82 and W112. Maximal membrane binding affinity is -11 kcal/mol (Hong et al. 2002), which is much higher than calculated transfer energy probably due to strong specific binding of sphingomyelin (Anderluh et al. 2005). This protein undergoes major conformational changes and oligomerization upon asociation with membranes.
2 references
Anderluh, G., Razpotnik, A., Podlesek, Z., Macek, P., Separovic, F., and Norton, R.S. 2005. Interaction of the eukaryotic pore-forming cytolysin equinatoxin II with model membranes: 19F NMR studies. J. Mol. Biol. 347:27-39. PubMed
Hong Q, Gutierrez-Aguirre I, Barlic A, Malovrh P, Kristan K, Podlesek Z, Macek P, Turk D, Gonzalez-Manas JM, Lakey JH, Anderluh G. 2002. Two-step membrane binding by Equinatoxin II, a pore-forming toxin from the sea anemone, involves an exposed aromatic cluster and a flexible helix. J Biol Chem. 277: 41916-41924. PubMed
Comments on 1iaz » Equinatoxin II
The protein has a cavity that may be involved in specific lipid binding.