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

Anticodon-binding domain swapping in a nondiscriminating aspartyl-tRNA synthetase reveals contributions to tRNA specificity and catalytic activity.

Proteins - 1 Sept 2020

Chuawong Pitak, Likittrakulwong Wirot, Suebka Suwimon, Wiriyatanakorn Nuttapon, Saparpakorn Patchreenart, Taweesablamlert Amata, Sudprasert Wanwisa, Hendrickson Tamara, Svasti Jisnuson

Abstract excerpt

The nondiscriminating aspartyl-tRNA synthetase (ND-AspRS), found in many archaea and bacteria, covalently attaches aspartic acid to tRNAAsp and tRNAAsn generating a correctly charged Asp-tRNAAsp and an erroneous Asp-tRNAAsn . This relaxed tRNA specificity is governed by interactions between the tRNA and the enzyme. In an effort to assess the contributions of the anticodon-binding domain to tRNA specificity, we...

Read the complete abstract on PubMed

Topics

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

Share to Anticodon
Share to Aspartate-tRNA Ligase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biocatalysis

Share to Helicobacter pylori

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to RNA, Transfer, Amino Acyl

Source

Identifiers

PMID: 32067260
DOI: 10.1002/prot.25881

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Anticodon-binding domain swapping in a nondiscriminating aspartyl-tRNA synthetase reveals contributions to tRNA specificity and catalytic activity.PMID 32067260Read ↗

A non-discriminating aspartyl-tRNA synthetase from Halobacterium salinarum.Semantic proximity Read ↗

Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms.Semantic proximity Read ↗

Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo.Semantic proximity Read ↗

Divergent anticodon recognition in contrasting glutamyl-tRNA synthetases.Semantic proximity Read ↗

Substrate specificity and catalysis by the editing active site of Alanyl-tRNA synthetase from Escherichia coli.Semantic proximity Read ↗

Yeast aspartyl-tRNA synthetase residues interacting with tRNA(Asp) identity bases connectively contribute to tRNA(Asp) binding in the ground and transition-state complex and discriminate against non-cognate tRNAs.Semantic proximity Read ↗

Distinct ways of G:U recognition by conserved tRNA binding motifs.Semantic proximity Read ↗

The identity determinants required for the discrimination between tRNAGlu and tRNAAsp by glutamyl-tRNA synthetase from Escherichia coli.Semantic proximity Read ↗

Human <i>trans</i> -editing enzyme displays tRNA acceptor stem specificity and relaxed amino acid selectivitySemantic proximity Read ↗

Role for a conserved structural motif in assembly of a class I aminoacyl-tRNA synthetase active site.Semantic proximity Read ↗

Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.Semantic proximity Read ↗

Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase.Semantic proximity Read ↗

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