Cloned (Comment) | Organism |
---|---|
expression in Bacillus megaterium | Clostridioides difficile |
Crystallization (Comment) | Organism |
---|---|
crystal structures of the toxin A glucosyltransferase domain in the presence and absence of the co-substrate UDP-alpha-D-glucose, to 2.2 and 2.6 A resolution, respectively | Clostridioides difficile |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | toxin A undergoes autocatalytic processing. The glucosyltransferase activity of the TcdA(1-1832) protein is activated by autoproteolysis. The presence of the autoprotease domain, residues 543-800, is restricting the activity of the glucosyl transferase domain | Clostridioides difficile |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + Rap2A | Clostridioides difficile | modification occurs in vitro and in cells | UDP + D-glucosyl-Rap2A | - |
? | |
UDP-alpha-D-glucose + Rap2A | Clostridioides difficile 630 | modification occurs in vitro and in cells | UDP + D-glucosyl-Rap2A | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridioides difficile | Q189K5 | toxin A | - |
Clostridioides difficile 630 | Q189K5 | toxin A | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | toxin A undergoes autocatalytic processing. The glucosyltransferase activity of the TcdA(1-1832) protein is activated by autoproteolysis. The presence of the autoprotease domain, residues 543-800, is restricting the activity of the glucosyl transferase domain | Clostridioides difficile |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + Cdc42 | - |
Clostridioides difficile | UDP + D-glucosyl-Cdc42 | - |
? | |
UDP-alpha-D-glucose + Cdc42 | - |
Clostridioides difficile 630 | UDP + D-glucosyl-Cdc42 | - |
? | |
UDP-alpha-D-glucose + Rac1 | - |
Clostridioides difficile | UDP + D-glucosyl-Rac1 | - |
? | |
UDP-alpha-D-glucose + Rac1 | - |
Clostridioides difficile 630 | UDP + D-glucosyl-Rac1 | - |
? | |
UDP-alpha-D-glucose + Rap2A | modification occurs in vitro and in cells | Clostridioides difficile | UDP + D-glucosyl-Rap2A | - |
? | |
UDP-alpha-D-glucose + Rap2A | modification occurs in vitro and in cells | Clostridioides difficile 630 | UDP + D-glucosyl-Rap2A | - |
? | |
UDP-alpha-D-glucose + RhoA | - |
Clostridioides difficile | UDP + D-glucosyl-RhoA | - |
? | |
UDP-alpha-D-glucose + RhoA | - |
Clostridioides difficile 630 | UDP + D-glucosyl-RhoA | - |
? |