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Literature summary for 2.4.1.B62 extracted from

  • Varela Chavez, C.; Haustant, G.M.; Baron, B.; England, P.; Chenal, A.; Pauillac, S.; Blondel, A.; Popoff, M.R.
    The tip of the four N-terminal alpha-helices of Clostridium sordellii lethal toxin contains the interaction site with membrane phosphatidylserine facilitating small GTPases glucosylation (2016), Toxins, 8, 90.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Paeniclostridium sordellii

Protein Variants

Protein Variants Comment Organism
F17K mutation strongly decreases binding to brain phosphatidylserine Paeniclostridium sordellii
K11I mutation moderately decreases binding to brain phosphatidylserine Paeniclostridium sordellii
K16I mutation moderately decreases binding to brain phosphatidylserine Paeniclostridium sordellii
Q10A mutation does not significantly decrease binding to brain phosphatidylserine Paeniclostridium sordellii
Q20A mutation moderately decreases binding to brain phosphatidylserine Paeniclostridium sordellii
R18P mutation strongly decreases binding to brain phosphatidylserine Paeniclostridium sordellii
R68A mutation strongly decreases binding to brain phosphatidylserine Paeniclostridium sordellii
S38A mutation does not significantly decrease binding to brain phosphatidylserine Paeniclostridium sordellii
V15S mutation strongly decreases binding to brain phosphatidylserine Paeniclostridium sordellii
Y14A mutation strongly decreases binding to brain phosphatidylserine Paeniclostridium sordellii
Y78A mutation does not significantly decrease binding to brain phosphatidylserine Paeniclostridium sordellii

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Paeniclostridium sordellii V5T923
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-

Synonyms

Synonyms Comment Organism
TcsL
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Paeniclostridium sordellii

General Information

General Information Comment Organism
physiological function the phosphatidylserine binding site is localized on the tip of the N-terminal four-helix bundle which is rich in positively-charged amino acids. Residues Y14, V15, F17, and R18 on loop 1, between helices 1 and 2, in coordination with R68 from loop 3, between helices 3 and 4, form a pocket which accommodates L-serine. The functional phosphatidylserine-binding site is required for N-terminal glucosylating domain TcsL-cat binding to the plasma membrane and subsequent cytotoxicity. TcsL-cat binding to phosphatidylserine facilitates a high enzymatic activity towards membrane-anchored Ras by about three orders of magnitude as compared to Ras in solution Paeniclostridium sordellii