ArticleThe EMBO journal2005
Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
- Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used.Life science alliance · 2023Article
- Discovery, Preclinical Characterization, and Early Clinical Activity of JDQ443, a Structurally Novel, Potent, and Selective Covalent Oral Inhibitor of KRASG12C.Cancer discovery · 2022Article
- A Coarse-Grained Methodology Identifies Intrinsic Mechanisms That Dissociate Interacting Protein Pairs.Frontiers in molecular biosciences · 2020Article
- Article
- Rho GTPase Recognition by C3 Exoenzyme Based on C3-RhoA Complex Structure.The Journal of biological chemistry · 2015Article
- Clostridial C3 Toxins Target Monocytes/Macrophages and Modulate Their Functions.Frontiers in immunology · 2015Review
- Article
- Novel bacterial ADP-ribosylating toxins: structure and function.Nature reviews. Microbiology · 2014Review
- Bacterial factors exploit eukaryotic Rho GTPase signaling cascades to promote invasion and proliferation within their host.Small GTPases · 2014Review
- Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.Molecular aspects of medicine · 2013Review
- A recombinant fusion toxin based on enzymatic inactive C3bot1 selectively targets macrophages.PloS one · 2013Article
- The 1.8 Å cholix toxin crystal structure in complex with NAD+ and evidence for a new kinetic model.The Journal of biological chemistry · 2012Article
- Identification and characterisation of the RalA-ERp57 interaction: evidence for GDI activity of ERp57.PloS one · 2012Article
- Bacterial protein toxins that modify host regulatory GTPases.Nature reviews. Microbiology · 2011Review
- Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases.PLoS computational biology · 2010Article
- C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins.Naunyn-Schmiedeberg's archives of pharmacology · 2007Review
- Cell Entry of C3 Exoenzyme from Clostridium botulinum.Current topics in microbiology and immunologyReview
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 binding of NAD and NAD-glycohydrolase activity remain. Here we report the crystal structure of C3 from C. botulinum in a complex with GDP-bound RalA at 1.8 A resolution. C3 binds RalA with a helix-loop-helix motif that is adjacent to the active site. A quaternary complex with NAD suggests a mode for ADP-ribosyltransferase inhibition. Interaction of C3 with RalA occurs at a unique interface formed by the switch-II region, helix alpha3 and the P loop of the GTPase. C3-binding stabilizes the GDP-bound conformation of RalA and blocks nucleotide release. Our data indicate that C. botulinum exoenzyme C3 is a single-domain toxin with bifunctional properties targeting Rho GTPases by ADP ribosylation and Ral by a guanine nucleotide dissociation inhibitor-like effect, which blocks nucleotide exchange.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.