4TR5

C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae

4TR5 の概要

• エントリーDOI: 10.2210/pdb4tr5/pdb
• 分子名称: C3larvin (2 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Paenibacillus larvae subsp. larvae BRL-230010
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24699.22

構造登録者

Ravulapalli, R.,Krska, D.,Merrill, A.R. (登録日: 2014-06-14, 公開日: 2014-12-17, 最終更新日: 2023-09-27)

主引用文献

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

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: 25477523
DOI: 10.1074/jbc.M114.589846

実験手法

X-RAY DIFFRACTION (2.3 Å)