3w9p

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'''Unreleased structure'''
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{{STRUCTURE_3w9p| PDB=3w9p | SCENE= }}
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===Crystal structure of monomeric FraC (second crystal form)===
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{{ABSTRACT_PUBMED_21300287}}
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The entry 3w9p 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: Caaveiro, J.M.M., Tanaka, K., Tsumoto, K.
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==About this Structure==
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[[3w9p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W9P OCA].
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Description: Crystal structure of monomeric FraC (second crystal 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: Caaveiro, J M.M.]]
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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: Cytolysin]]
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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 06:34, 9 April 2014

Template:STRUCTURE 3w9p

Contents

Crystal structure of monomeric FraC (second crystal 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

3w9p is a 2 chain structure. 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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