4tr5

C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae

spinqualitylabelsall models 4tr5, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tr5 is a 1 chain structure with sequence from Paenibacillus larvae subsp. larvae BRL-230010. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W2E3J5_9BACL Publication Abstract from PubMed 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 muM) and RhoA (KM, 17 +/- 3 muM) substrates were characterized for this enzyme from the mART 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 it lethality through its enzyme activity. A small molecule inhibitor of C3larvin enzymatic activity was discovered called M3 (Ki = 11 +/- 2 muM), and to our knowledge is the first inhibitor of transferase activity of the C3 toxin family. C3larvin was crystallized, and its crystal structure (apo-enzyme) was solved to 2.3 A resolution. C3larvin was also shown to have a different mechanism of cell entry from other C3 toxins. C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae.,Krska D, Ravulapalli R, Fieldhouse RJ, Lugo MR, Merrill AR J Biol Chem. 2014 Dec 4. pii: jbc.M114.589846. PMID:25477523 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA