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

Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain.

Structure (London, England : 1993) - 1 Apr 2008

Benarroch Delphine, Smith Paul, Shuman Stewart

Abstract excerpt

The RNA triphosphatase (RTPase) components of the mRNA capping apparatus are a bellwether of eukaryal taxonomy. Fungal and protozoal RTPases belong to the triphosphate tunnel metalloenzyme (TTM) family, exemplified by yeast Cet1. Several large DNA viruses encode metal-dependent RTPases unrelated to the cysteinyl-phosphatase RTPases of their metazoan host organisms. The origins of DNA virus RTPases are unclear...

Read the complete abstract on PubMed

Topics

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

Share to Acid Anhydride Hydrolases
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Viruses

Share to Methyltransferases

Share to Nucleotidyltransferases

Share to Protein Structure, Tertiary

Share to Sequence Alignment

Share to Viral Proteins

Source

Identifiers

PMID: 18400173
DOI: 10.1016/j.str.2008.01.009

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain.PMID 18400173Read ↗

Mapping the triphosphatase active site of baculovirus mRNA capping enzyme LEF4 and evidence for a two-metal mechanism.Semantic proximity Read ↗

Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus.Semantic proximity Read ↗

Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus.Semantic proximity Read ↗

Novel triphosphate phosphohydrolase activity of Clostridium thermocellum TTM, a member of the triphosphate tunnel metalloenzyme superfamily.Semantic proximity Read ↗

RNA triphosphatase-mediated mRNA capping is essential for maintaining transcript homeostasis and the survival of Toxoplasma gondiiSemantic proximity Read ↗

RNA triphosphatase-mediated mRNA capping is essential for maintaining transcript homeostasis and the survival of Toxoplasma gondiiSemantic proximity Read ↗

Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active site.Semantic proximity Read ↗

Functional groups required for the stability of yeast RNA triphosphatase in vitro and in vivo.Semantic proximity Read ↗

RNA-editing terminal uridylyl transferase 1: identification of functional domains by mutational analysis.Semantic proximity Read ↗

A yeast-based genetic system for functional analysis of viral mRNA capping enzymes.Semantic proximity Read ↗

Structure and mechanism of a metal-sensing regulatory RNA.Semantic proximity Read ↗

Comparative genomics and evolution of proteins involved in RNA metabolism.Semantic proximity Read ↗

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