5ec5
From Proteopedia
Crystal structure of lysenin pore
Structural highlights
FunctionTXL_EISFE Pore-forming toxin that specifically binds sphingomyelin in the plasma membrane of various cells. Has hemolytic activity. Is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells. Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction. It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10 times more effective than lysenin-related protein 1.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedThe invertebrate cytolysin lysenin is a member of the aerolysin family of pore-forming toxins that includes many representatives from pathogenic bacteria. Here we report the crystal structure of the lysenin pore and provide insights into its assembly mechanism. The lysenin pore is assembled from nine monomers via dramatic reorganization of almost half of the monomeric subunit structure leading to a beta-barrel pore approximately 10 nm long and 1.6-2.5 nm wide. The lysenin pore is devoid of additional luminal compartments as commonly found in other toxin pores. Mutagenic analysis and atomic force microscopy imaging, together with these structural insights, suggest a mechanism for pore assembly for lysenin. These insights are relevant to the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represent crucial virulence factors in bacteria. Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.,Podobnik M, Savory P, Rojko N, Kisovec M, Wood N, Hambley R, Pugh J, Wallace EJ, McNeill L, Bruce M, Liko I, Allison TM, Mehmood S, Yilmaz N, Kobayashi T, Gilbert RJ, Robinson CV, Jayasinghe L, Anderluh G Nat Commun. 2016 May 12;7:11598. doi: 10.1038/ncomms11598. PMID:27176125[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Eisenia fetida | Large Structures | Anderluh G | Bruce M | Jayasinghe L | Kisovec M | Podobnik M | Rojko N | Savory P
