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1iaz

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[[Image:1iaz.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iaz OCA], [http://www.ebi.ac.uk/pdbsum/1iaz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iaz RCSB]</span>
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'''EQUINATOXIN II'''
'''EQUINATOXIN II'''
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[[Category: Macek, P.]]
[[Category: Macek, P.]]
[[Category: Turk, D.]]
[[Category: Turk, D.]]
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[[Category: beta-sandwich]]
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[[Category: Beta-sandwich]]
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Revision as of 16:47, 2 May 2008

Template:STRUCTURE 1iaz

EQUINATOXIN II


Overview

BACKGROUND: Membrane pore-forming toxins have a remarkable property: they adopt a stable soluble form structure, which, when in contact with a membrane, undergoes a series of transformations, leading to an active, membrane-bound form. In contrast to bacterial toxins, no structure of a pore-forming toxin from an eukaryotic organism has been determined so far, an indication that structural studies of equinatoxin II (EqtII) may unravel a novel mechanism. RESULTS: The crystal structure of the soluble form of EqtII from the sea anemone Actinia equina has been determined at 1.9 A resolution. EqtII is shown to be a single-domain protein based on a 12 strand beta sandwich fold with a hydrophobic core and a pair of alpha helices, each of which is associated with the face of a beta sheet. CONCLUSIONS: The structure of the 30 N-terminal residues is the largest segment that can adopt a different structure without disrupting the fold of the beta sandwich core. This segment includes a three-turn alpha helix that lies on the surface of a beta sheet and ends in a stretch of three positively charged residues, Lys-30, Arg-31, and Lys-32. On the basis of gathered data, it is suggested that this segment forms the membrane pore, whereas the beta sandwich structure remains unaltered and attaches to a membrane as do other structurally related extrinsic membrane proteins or their domains. The use of a structural data site-directed mutagenesis study should reveal the residues involved in membrane pore formation.

About this Structure

1IAZ is a Single protein structure of sequence from Actinia equina. Full crystallographic information is available from OCA.

Reference

Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina., Athanasiadis A, Anderluh G, Macek P, Turk D, Structure. 2001 Apr 4;9(4):341-6. PMID:11525171 Page seeded by OCA on Fri May 2 19:47:24 2008

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