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1kd6

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{{STRUCTURE_1kd6| PDB=1kd6 | SCENE= }}
{{STRUCTURE_1kd6| PDB=1kd6 | SCENE= }}
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'''Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II'''
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===Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II===
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==Overview==
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Sea anemones produce a family of 18-20 kDa proteins, the actinoporins, that lyse cells by forming pores in cell membranes. Sphingomyelin plays an important role in their lytic activity, with membranes lacking this lipid being largely refractory to these toxins. The structure of the actinoporin equinatoxin II in aqueous solution, determined from NMR data, consists of two short helices packed against opposite faces of a beta-sandwich structure formed by two five-stranded beta-sheets. The protein core has extensive hydrophobic interfaces formed by residues projecting from the internal faces of the two beta-sheets. 15N relaxation data show uniform backbone dynamics, implying that equinatoxin II in solution is relatively rigid, except at the N terminus; its inferred rotational correlation time is consistent with values for monomeric proteins of similar mass. Backbone amide exchange rate data also support the view of a stable structure, even though equinatoxin II lacks disulfide bonds. As monitored by NMR, it unfolds at around 70 degrees C at pH 5.5. At 25 degrees C the structure is stable over the pH range 2.5-7.3 but below pH 2.5 it undergoes a slow transition to an incompletely unfolded structure resembling a molten globule. Equinatoxin II has two significant patches of positive electrostatic potential formed by surface-exposed Lys and Arg residues, which may assist its interaction with charged regions of the lipid head groups. Tyr and Trp residues on the surface may also contribute by interacting with the carbonyl groups of the acyl chains of target membranes. Data from mutational studies and truncated analogues identify two regions of the protein involved in membrane interactions, the N-terminal helix and the Trp-rich region. Once the protein is anchored, the N-terminal helix may penetrate the membrane, with up to four helices lining the pore, although other mechanisms of pore formation cannot be ruled out.
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(as it appears on PubMed at http://www.pubmed.gov), where 11827489 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11827489}}
==About this Structure==
==About this Structure==
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1KD6 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=1KD6 OCA].
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1KD6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Actinia_equina Actinia equina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KD6 OCA].
==Reference==
==Reference==
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[[Category: Sea anemone]]
[[Category: Sea anemone]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:35:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:09:36 2008''

Revision as of 07:09, 2 July 2008

Image:1kd6.png

Template:STRUCTURE 1kd6

Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II

Template:ABSTRACT PUBMED 11827489

About this Structure

1KD6 is a Single protein structure of sequence from Actinia equina. Full experimental information is available from OCA.

Reference

Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation., Hinds MG, Zhang W, Anderluh G, Hansen PE, Norton RS, J Mol Biol. 2002 Feb 1;315(5):1219-29. PMID:11827489

Page seeded by OCA on Wed Jul 2 10:09:36 2008

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