1tzq: Difference between revisions
No edit summary |
No edit summary |
||
Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1iaz|1IAZ]] | |||
|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> | |||
}} | }} | ||
Line 33: | Line 36: | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:03:22 2008'' |
Revision as of 00:03, 31 March 2008
| |||||||
, 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
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
Page seeded by OCA on Mon Mar 31 00:03:22 2008