4TR5
C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae
Summary for 4TR5
| Entry DOI | 10.2210/pdb4tr5/pdb |
| Descriptor | C3larvin (2 entities in total) |
| Functional Keywords | transferase |
| Biological source | Paenibacillus larvae subsp. larvae BRL-230010 |
| Total number of polymer chains | 1 |
| Total formula weight | 24699.22 |
| Authors | Ravulapalli, R.,Krska, D.,Merrill, A.R. (deposition date: 2014-06-14, release date: 2014-12-17, Last modification date: 2023-09-27) |
| Primary citation | Krska, D.,Ravulapalli, R.,Fieldhouse, R.J.,Lugo, M.R.,Merrill, A.R. C3larvin Toxin, an ADP-ribosyltransferase from Paenibacillus larvae. J.Biol.Chem., 290:1639-1653, 2015 Cited by PubMed Abstract: C3larvin toxin was identified by a bioinformatic strategy as a putative mono-ADP-ribosyltransferase and a possible virulence factor from Paenibacillus larvae, which is the causative agent of American Foulbrood in honey bees. C3larvin targets RhoA as a substrate for its transferase reaction, and kinetics for both the NAD(+) (Km = 34 ± 12 μm) and RhoA (Km = 17 ± 3 μm) substrates were characterized for this enzyme from the mono-ADP-ribosyltransferase C3 toxin subgroup. C3larvin is toxic to yeast when expressed in the cytoplasm, and catalytic variants of the enzyme lost the ability to kill the yeast host, indicating that the toxin exerts its lethality through its enzyme activity. A small molecule inhibitor of C3larvin enzymatic activity was discovered called M3 (Ki = 11 ± 2 μm), and to our knowledge, is the first inhibitor of transferase activity of the C3 toxin family. C3larvin was crystallized, and its crystal structure (apoenzyme) was solved to 2.3 Å resolution. C3larvin was also shown to have a different mechanism of cell entry from other C3 toxins. PubMed: 25477523DOI: 10.1074/jbc.M114.589846 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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