3vwi
High resolution crystal structure of FraC in the monomeric formHigh resolution crystal structure of FraC in the monomeric form
Template:ABSTRACT PUBMED 21300287
FunctionFunction
[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 StructureAbout this Structure
3vwi is a 4 chain structure with sequence from Actinia fragacea. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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
- ↑ 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