Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme.

Abstract

C3 exoenzymes from bacterial pathogens ADP-ribosylate and inactivate low-molecular-mass GTPases of the Rho subfamily. Ral, a Ras subfamily GTPase, binds the C3 exoenzymes from Clostridium botulinum and C. limosum with high affinity without being a substrate for ADP ribosylation. In the complex, the ADP-ribosyltransferase activity of C3 is blocked, while… (More)

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Cite this paper

@article{Pautsch2005CrystalSO, title={Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme.}, author={Alexander Pautsch and Martin Vogelsgesang and Jens Traenkle and Christian Herrmann and Klaus Aktories}, journal={The EMBO journal}, year={2005}, volume={24 20}, pages={3670-80} }