Crystal structure of the Clostridium limosum C3 exoenzyme

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 crysta...

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Veröffentlicht in:FEBS letters 2008-04, Vol.582 (7), p.1032-1036
Hauptverfasser: Vogelsgesang, Martin, Stieglitz, Benjamin, Herrmann, Christian, Pautsch, Alex, Aktories, Klaus
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Sprache:eng
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Zusammenfassung: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 1.8 Å 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2008.02.051