3vwi: Difference between revisions

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{{STRUCTURE_3vwi|  PDB=3vwi  |  SCENE=  }}
==High resolution crystal structure of FraC in the monomeric form==
===High resolution crystal structure of FraC in the monomeric form===
<StructureSection load='3vwi' size='340' side='right' caption='[[3vwi]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
{{ABSTRACT_PUBMED_21300287}}
== Structural highlights ==
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VWI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lim|3lim]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FraC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=396334 Actinia fragacea])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vwi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vwi RCSB], [http://www.ebi.ac.uk/pdbsum/3vwi PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 A resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free alpha-helical bundle pore.


==Function==
Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins.,Mechaly AE, Bellomio A, Gil-Carton D, Morante K, Valle M, Gonzalez-Manas JM, Guerin DM Structure. 2011 Feb 9;19(2):181-91. PMID:21300287<ref>PMID:21300287</ref>
[[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>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[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].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021300287</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Actinia fragacea]]
[[Category: Actinia fragacea]]
[[Category: Caaveiro, J M.M.]]
[[Category: Caaveiro, J M.M]]
[[Category: Gonzalez-Manas, J M.]]
[[Category: Gonzalez-Manas, J M]]
[[Category: Morante, K.]]
[[Category: Morante, K]]
[[Category: Tanaka, K.]]
[[Category: Tanaka, K]]
[[Category: Tsumoto, K.]]
[[Category: Tsumoto, K]]
[[Category: Actinoporin]]
[[Category: Actinoporin]]
[[Category: Amphipathic alpha-helix]]
[[Category: Amphipathic alpha-helix]]

Revision as of 09:56, 21 December 2014

High resolution crystal structure of FraC in the monomeric formHigh resolution crystal structure of FraC in the monomeric form

Structural highlights

3vwi is a 4 chain structure with sequence from Actinia fragacea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:FraC (Actinia fragacea)
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 A resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free alpha-helical bundle pore.

Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins.,Mechaly AE, Bellomio A, Gil-Carton D, Morante K, Valle M, Gonzalez-Manas JM, Guerin DM Structure. 2011 Feb 9;19(2):181-91. PMID:21300287[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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

3vwi, resolution 1.70Å

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