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 and mutational analysis of archaeal ATP-dependent RNA ligase identifies amino acids required for RNA binding and catalysis.

Nucleic acids research - 18 Mar 2016

Gu Huiqiong, Yoshinari Shigeo, Ghosh Raka, Ignatochkina Anna V, Gollnick Paul D, Murakami Katsuhiko S, Ho C Kiong

Abstract excerpt

An ATP-dependent RNA ligase from Methanobacterium thermoautotrophicum (MthRnl) catalyzes intramolecular ligation of single-stranded RNA to form a closed circular RNA via covalent ligase-AMP and RNA-adenylylate intermediate. Here, we report the X-ray crystal structures of an MthRnl•ATP complex as well as the covalent MthRnl-AMP intermediate. We also performed structure-guided mutational analysis to survey the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Archaeal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biocatalysis

Share to Crystallography, X-Ray

Share to Protein Structure, Secondary

Share to RNA, Archaeal

Share to RNA, Circular

Source

Open in PubMed Open full text

Identifiers

PMID: 26896806
DOI: 10.1093/nar/gkw094
PMCID: PMC4797309

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

Structural and mutational analysis of archaeal ATP-dependent RNA ligase identifies amino acids required for RNA binding and catalysis.PMID 26896806Read ↗

Characterisation and engineering of a thermophilic RNA ligase from Palaeococcus pacificus.Semantic proximity Read ↗

Mutational analysis of bacteriophage T4 RNA ligase 1. Different functional groups are required for the nucleotidyl transfer and phosphodiester bond formation steps of the ligation reaction.Semantic proximity Read ↗

Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining.Semantic proximity Read ↗

Characterization of an ATP-dependent DNA ligase from the thermophilic archaeon Methanobacterium thermoautotrophicum.Semantic proximity Read ↗

Structure and mechanism of RNA ligase.Semantic proximity Read ↗

NAD+-dependent DNA Ligase (Rv3014c) from Mycobacterium tuberculosis. Crystal structure of the adenylation domain and identification of novel inhibitors.Semantic proximity Read ↗

The closed structure of an archaeal DNA ligase from Pyrococcus furiosus.Semantic proximity Read ↗

Biochemical and structural insights into a 5’ to 3’ RNA ligase reveal a potential role in tRNA ligationSemantic proximity Read ↗

Mutational, structural, and kinetic studies of the ATP-binding site of Methanobacterium thermoautotrophicum nicotinamide mononucleotide adenylyltransferase.Semantic proximity Read ↗

Structure-function analysis of T4 RNA ligase 2.Semantic proximity Read ↗

Insights into ligand binding and catalysis of a central step in NAD+ synthesis: structures of Methanobacterium thermoautotrophicum NMN adenylyltransferase complexes.Semantic proximity Read ↗

An RNA ligase from Deinococcus radiodurans.Semantic proximity Read ↗

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