1tzq: Difference between revisions
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[[Image:1tzq.gif|left|200px]] | [[Image:1tzq.gif|left|200px]] | ||
'''Crystal structure of the equinatoxin II 8-69 double cysteine mutant''' | {{Structure | ||
|PDB= 1tzq |SIZE=350|CAPTION= <scene name='initialview01'>1tzq</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''Crystal structure of the equinatoxin II 8-69 double cysteine mutant''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TZQ is a [ | 1TZQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Actinia_equina Actinia equina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZQ OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15322132 15322132] | ||
[[Category: Actinia equina]] | [[Category: Actinia equina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:25:23 2008'' | ||
Revision as of 15:25, 20 March 2008
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Crystal structure of the equinatoxin II 8-69 double cysteine mutant
OverviewOverview
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 StructureAbout this Structure
1TZQ is a Single protein structure of sequence from Actinia equina. Full crystallographic information is available from OCA.
ReferenceReference
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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