Structural highlights
Function
ARC3_HATLI ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue.[UniProtKB:P15879]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
C3-like toxins ADP-ribosylate and inactivate Rho GTPases. Seven C3-like ADP-ribosyltransferases produced by Clostridium botulinum, Clostridium limosum, Bacillus cereus and Staphylococcus aureus were identified and two representatives--C3bot from C. botulinum and C3stau2 from S. aureus--were crystallized. Here we present the 1.8A structure of C. limosum C3 transferase C3lim and compare it to the structures of other family members. In contrast to the structure of apo-C3bot, the canonical ADP-ribosylating turn turn motif is observed in a primed conformation, ready for NAD binding. This suggests an impact on the binding mode of NAD and on the transferase reaction. The crystal structure explains why auto-ADP-ribosylation of C3lim at Arg41 interferes with the ADP-ribosyltransferase activity of the toxin.
Crystal structure of the Clostridium limosum C3 exoenzyme.,Vogelsgesang M, Stieglitz B, Herrmann C, Pautsch A, Aktories K FEBS Lett. 2008 Apr 2;582(7):1032-6. Epub 2008 Mar 4. PMID:18325337[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vogelsgesang M, Stieglitz B, Herrmann C, Pautsch A, Aktories K. Crystal structure of the Clostridium limosum C3 exoenzyme. FEBS Lett. 2008 Apr 2;582(7):1032-6. Epub 2008 Mar 4. PMID:18325337 doi:10.1016/j.febslet.2008.02.051
