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

Structure of anthrax edema factor-calmodulin-adenosine 5'-(alpha,beta-methylene)-triphosphate complex reveals an alternative mode of ATP binding to the catalytic site.

Biochemical and biophysical research communications - 30 Apr 2004

Shen Yuequan, Guo Qing, Zhukovskaya Natalia L, Drum Chester L, Bohm Andrew, Tang Wei-Jen

Abstract excerpt

Anthrax edema factor (EF) is a key virulence factor secreted by Bacillus anthracis. Here, we report a structure, at 3.0 A resolution, of the catalytic domain of EF (EF3) in complex with calmodulin (CaM) and adenosine 5'-(alpha,beta-methylene)-triphosphate (AMPCPP). Although the binding of the triphosphate of AMPCPP to EF3 can be superimposed on that of previously determined 3'deoxy-ATP (3'dATP) and 2'deoxy 3'...

Read the complete abstract on PubMed

Topics

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

Share to Adenylyl Cyclases
Share to Antigens, Bacterial

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Bacterial Toxins

Share to Calmodulin

Share to Catalysis

Share to Coenzymes

Share to Macromolecular Substances

Share to Molecular Conformation

Source

Identifiers

PMID: 15063758
DOI: 10.1016/j.bbrc.2004.03.046

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure of anthrax edema factor-calmodulin-adenosine 5'-(alpha,beta-methylene)-triphosphate complex reveals an alternative mode of ATP binding to the catalytic site.PMID 15063758Read ↗

MD simulations of anthrax edema factor: calmodulin complexes with mutations in the edema factor "switch a" region and docking of 3'-deoxy ATP into the adenylyl cyclase active site of wild-type and mutant edema factor variants.Semantic proximity Read ↗

An extended conformation of calmodulin induces interactions between the structural domains of adenylyl cyclase from Bacillus anthracis to promote catalysis.Semantic proximity Read ↗

Inhibition of the adenylyl cyclase toxin, edema factor, from Bacillus anthracis by a series of 18 mono- and bis-(M)ANT-substituted nucleoside 5'-triphosphates.Semantic proximity Read ↗

Kinetic characterization and ligand binding studies of His351 mutants of Bacillus anthracis adenylate cyclase.Semantic proximity Read ↗

Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins.Semantic proximity Read ↗

Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin.Semantic proximity Read ↗

A-type ATP binding consensus sequences are critical for the catalytic activity of the calmodulin-sensitive adenylyl cyclase from Bacillus anthracis.Semantic proximity Read ↗

Solution structure of an ATP-binding RNA aptamer reveals a novel fold.Semantic proximity Read ↗

Conserved inhibitory mechanism and competent ATP binding mode for adenylyltransferases with Fic fold.Semantic proximity Read ↗

Mapping the anthrax protective antigen binding site on the lethal and edema factors.Semantic proximity Read ↗

Crystal structure of Bacillus anthracis virulence regulator AtxA and effects of phosphorylated histidines on multimerization and activity.Semantic proximity Read ↗

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

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