Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes.

Protein science : a publication of the Protein Society - 1 May 2008

Ménétrey Julie, Flatau Gilles, Boquet Patrice, Ménez André, Stura Enrico A

Abstract excerpt

C3-like exoenzymes are ADP-ribosyltransferases that specifically modify some Rho GTPase proteins, leading to their sequestration in the cytoplasm, and thus inhibiting their regulatory activity on the actin cytoskeleton. This modification process goes through three sequential steps involving NAD-h...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ADP Ribose Transferases
Share to Amino Acid Substitution
Share to Asparagine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Botulinum Toxins

Share to Crystallography, X-Ray

Share to Glutamic Acid

Share to Hydrolysis

Source

Open in PubMed Open full text

Identifiers

PMID: 18369192
DOI: 10.1110/ps.073398508
PMCID: PMC2327275

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-18369192-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes.PMID 18369192Read ↗

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

Structural basis of actin recognition and arginine ADP-ribosylation by <i>Clostridium perfringens</i> ι-toxinSemantic proximity Read ↗

Structural constraints-based evaluation of immunogenic avirulent toxins from Clostridium botulinum C2 and C3 toxins as subunit vaccines.Semantic proximity Read ↗

Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants.Semantic proximity Read ↗

Proteome Alterations of Hippocampal Cells Caused by Clostridium botulinum C3 Exoenzyme.Semantic proximity Read ↗

Unique structural and nucleotide exchange features of the Rho1 GTPase of Entamoeba histolytica.Semantic proximity Read ↗

The tRNA-modifying function of MnmE is controlled by post-hydrolysis steps of its GTPase cycle.Semantic proximity Read ↗

Structural insights into GDP-mediated regulation of a bacterial acyl-CoA thioesterase.Semantic proximity Read ↗

A Comprehensive Structural Analysis of Clostridium botulinum Neurotoxin A Cell-Binding Domain from Different SubtypesSemantic proximity Read ↗

Reflections on the catalytic power of a TIM-barrel.Semantic proximity Read ↗

Kinetic and structural insights into the mechanism of AMPylation by VopS Fic domain.Semantic proximity Read ↗

Crystal structure of E. coli apolipoprotein N-acyl transferase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.