Literature summary for 2.4.1.B62 extracted from

Varela Chavez, C.; Hoos, S.; Haustant, G.M.; Chenal, A.; England, P.; Blondel, A.; Pauillac, S.; Lacy, D.B.; Popoff, M.R.
The catalytic domains of Clostridium sordellii lethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid (2015), Cell. Microbiol., 17, 1477-1493.

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Organism

Organism	UniProt	Comment	Textmining
Paeniclostridium sordellii	V5T923	-	-

General Information

General Information	Comment	Organism
physiological function	isoform TcsL enters target cells via receptor-mediated endocytosis and delivers the N-terminal catalytic domain (TcsL-cat) into the cytosol. TcsL-cat binds to brain phosphatidylserine-containing membranes and to phosphatidic acid and, to a lesser extent, to other anionic lipids, but not to neutral lipids, sphingolipids or sterol. The lipid unsaturation status influences TcsL-cat binding to phospholipids, phosphatidylserines with unsaturated acyl chains and phosphatidic acids with saturated acyl chains being the preferred binding substrates. The phospholipid binding site is localized at the N-terminal four helical bundle structure (1-93 domain). Recombinant TcsL-1-93 binds to a broad range of substrates, whereas TcsL-cat, which is the active domain physiologically delivered into the cytosol, selectively binds to phosphatidylserine and phosphatidic acid	Paeniclostridium sordellii

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Release 2023.1 (January 2023)