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Crystal structure of the Clostridium limosum C3 exoenzyme
Author(s) -
Vogelsgesang Martin,
Stieglitz Benjamin,
Herrmann Christian,
Pautsch Alex,
Aktories Klaus
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.02.051
Subject(s) - exoenzyme , chemistry , food science , microbiology and biotechnology , biochemistry , biology , enzyme
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.