1tzq: Difference between revisions

Revision as of 12:51, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tzq.png

Template:STRUCTURE 1tzq

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

Template:ABSTRACT PUBMED 15322132

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1tzq.gif|left|200px]]
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-'''Crystal structure of the equinatoxin II 8-69 double cysteine mutant'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15322132}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15322132 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15322132}}
 ==About this Structure==
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 [[Category: Turk, D A.]]
 [[Category: Beta-sandwich]]
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