3vwi

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'''Unreleased structure'''
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{{STRUCTURE_3vwi| PDB=3vwi | SCENE= }}
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===High resolution crystal structure of FraC in the monomeric form===
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{{ABSTRACT_PUBMED_21300287}}
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The entry 3vwi is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/ACTPC_ACTFR ACTPC_ACTFR]] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers.<ref>PMID:19563820</ref>
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Authors: Tanaka, K., Morante, K., Caaveiro, J.M.M., Gonzalez-Manas, J.M., Tsumoto, K.
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==About this Structure==
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[[3vwi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinia_fragacea Actinia fragacea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VWI OCA].
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Description: High resolution crystal structure of FraC in the monomeric form
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==Reference==
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<ref group="xtra">PMID:021300287</ref><references group="xtra"/><references/>
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[[Category: Actinia fragacea]]
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[[Category: Caaveiro, J M.M.]]
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[[Category: Gonzalez-Manas, J M.]]
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[[Category: Morante, K.]]
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[[Category: Tanaka, K.]]
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[[Category: Tsumoto, K.]]
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[[Category: Actinoporin]]
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[[Category: Amphipathic alpha-helix]]
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[[Category: Beta-sandwich]]
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[[Category: Citolysin]]
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[[Category: Lipid raft]]
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[[Category: Membrane lipid]]
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[[Category: Pore-forming toxin]]
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[[Category: Secreted protein]]
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[[Category: Toxin]]

Revision as of 07:28, 28 August 2013

Template:STRUCTURE 3vwi

Contents

High resolution crystal structure of FraC in the monomeric form

Template:ABSTRACT PUBMED 21300287

Function

[ACTPC_ACTFR] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers.[1]

About this Structure

3vwi is a 4 chain structure with sequence from Actinia fragacea. Full crystallographic information is available from OCA.

Reference

  • Mechaly AE, Bellomio A, Gil-Carton D, Morante K, Valle M, Gonzalez-Manas JM, Guerin DM. Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins. Structure. 2011 Feb 9;19(2):181-91. PMID:21300287 doi:10.1016/j.str.2010.11.013
  1. ↑ Bellomio A, Morante K, Barlic A, Gutierrez-Aguirre I, Viguera AR, Gonzalez-Manas JM. Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea. Toxicon. 2009 Nov;54(6):869-80. doi: 10.1016/j.toxicon.2009.06.022. Epub 2009 Jun, 27. PMID:19563820 doi:10.1016/j.toxicon.2009.06.022

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