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1tzq

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzq OCA], [http://www.ebi.ac.uk/pdbsum/1tzq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tzq RCSB]</span>
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[[Category: beta-sandwich]]
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Revision as of 21:03, 30 March 2008


PDB ID 1tzq

Drag the structure with the mouse to rotate
, resolution 2.3Å
Related: 1IAZ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the equinatoxin II 8-69 double cysteine mutant


Overview

Actinoporins are eukaryotic pore-forming proteins that create 2-nm pores in natural and model lipid membranes by the self-association of four monomers. The regions that undergo conformational change and form part of the transmembrane pore are currently being defined. It was shown recently that the N-terminal region (residues 10-28) of equinatoxin, an actinoporin from Actinia equina, participates in building of the final pore wall. Assuming that the pore is formed solely by a polypeptide chain, other parts of the toxin should constitute the conductive channel and here we searched for these regions by disulfide scanning mutagenesis. Only double cysteine mutants where the N-terminal segment 1-30 was attached to the beta-sandwich exhibited reduced hemolytic activity upon disulfide formation, showing that other parts of equinatoxin, particularly the beta-sandwich and importantly the C-terminal alpha-helix, do not undergo large conformational rearrangements during the pore formation. The role of the beta-sandwich stability was independently assessed via destabilization of a part of its hydrophobic core by mutations of the buried Trp117. These mutants were considerably less stable than the wild-type but exhibited similar or slightly lower permeabilizing activity. Collectively these results show that a flexible N-terminal region and stable beta-sandwich are pre-requisite for proper pore formation by the actinoporin family.

About this Structure

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

Reference

Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich., Kristan K, Podlesek Z, Hojnik V, Gutierrez-Aguirre I, Guncar G, Turk D, Gonzalez-Manas JM, Lakey JH, Macek P, Anderluh G, J Biol Chem. 2004 Nov 5;279(45):46509-17. Epub 2004 Aug 20. PMID:15322132

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