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Article

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

The EMBO journal - 19 Oct 2005

Pautsch Alexander, Vogelsgesang Martin, Tränkle Jens, Herrmann Christian, Aktories Klaus

Abstract excerpt

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 binding of NAD and NAD-glycohydrolase activity remain. Here...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16177825
DOI: 10.1038/sj.emboj.7600813
PMCID: PMC1276701

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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