3BW8

Crystal structure of the Clostridium limosum C3 exoenzyme

Summary for 3BW8

• Entry DOI: 10.2210/pdb3bw8/pdb
• Related: 1GZE 1GZF 1OJQ 1OJZ
• Descriptor: Mono-ADP-ribosyltransferase C3, SULFATE ION (3 entities in total)
• Functional Keywords: c3lim, exoenzyme c3, adp-ribosyltransferase, rho, ribosylating toxin, artt, c3bot, c3cer, c3stau, glycosyltransferase, nad, secreted, transferase
• Biological source: Clostridium limosum
• Cellular location: Secreted: Q46134
• Total number of polymer chains: 2
• Total formula weight: 47914.15

Authors

Vogelsgesang, M.,Stieglitz, B.,Herrmann, C.,Pautsch, A.,Aktories, K. (deposition date: 2008-01-08, release date: 2008-04-01, Last modification date: 2023-08-30)

Primary citation

Vogelsgesang, M.,Stieglitz, B.,Herrmann, C.,Pautsch, A.,Aktories, K.
Crystal structure of the Clostridium limosum C3 exoenzyme.
Febs Lett., 582:1032-1036, 2008

PubMed Abstract: 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.

PubMed: 18325337
DOI: 10.1016/j.febslet.2008.02.051

Experimental method

X-RAY DIFFRACTION (1.8 Å)