DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ de-2012-10 in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined De Colibus L., Sonnen AF., Morris KJ., Siebert CA., Abrusci P., Plitzko J., Hodnik V., Leippe M., Volpi E., Anderluh G., Gilbert RJ. DIP original experiment: DIP-250510X Structure (London, England : 1993) 2012 IMEx Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition. De Colibus L., Sonnen AF., Morris KJ., Siebert CA., Abrusci P., Plitzko J., Hodnik V., Leippe M., Volpi E., Anderluh G., Gilbert RJ. Only protein-protein interactions imex curation txl_eisfe Lysenin Beta-barrel pore-forming toxin Invertebrate cytolysin pore efL1 protein protein eisfe Eisenia fetida Red wiggler worm MSAKAAEGYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQVSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIVGRQIILGKTEIRIKHAERKEYMTVVSRKSWPAATLGHSKLFKFVLYEDWGGFRIKTLNTMYSGYEYAYSSDQGGIYFDQGTDNPKQRWAINKSLPLRHGDVVTFMNKYFTRSGLCYDDGPATNVYCLDKREDKWILEVVG txl_eisfe-1 3242766 N/A 3242767 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false