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

Shape-selective RNA recognition by cysteinyl-tRNA synthetase.

Nature structural & molecular biology - 1 Nov 2004

Hauenstein Scott, Zhang Chun-Mei, Hou Ya-Ming, Perona John J

Abstract excerpt

The crystal structure of Escherichia coli cysteinyl-tRNA synthetase (CysRS) bound to tRNA(Cys) at a resolution of 2.3 A reveals base-specific and shape-selective interactions across an extensive protein-RNA recognition interface. The complex contains a mixed alpha/beta C-terminal domain, which is disordered in the unliganded enzyme. This domain makes specific hydrogen bonding interactions with all three bases of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acyl-tRNA Synthetases
Share to Catalytic Domain
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Fluorescence

Share to Nucleic Acid Conformation

Share to Phosphates

Share to RNA, Transfer

Source

Identifiers

PMID: 15489861
DOI: 10.1038/nsmb849

Genes

GCA

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

Shape-selective RNA recognition by cysteinyl-tRNA synthetase.PMID 15489861Read ↗

Anticodon recognition and discrimination by the alpha-helix cage domain of class I lysyl-tRNA synthetase.Semantic proximity Read ↗

Allosteric communication in cysteinyl tRNA synthetase: a network of direct and indirect readout.Semantic proximity Read ↗

Amino acid discrimination by a highly differentiated metal center of an aminoacyl-tRNA synthetase.Semantic proximity Read ↗

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

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

Tertiary core rearrangements in a tight binding transfer RNA aptamer.Semantic proximity Read ↗

Alternative design of a tRNA core for aminoacylation.Semantic proximity Read ↗

A strategy of tRNA recognition that includes determinants of RNA structure.Semantic proximity Read ↗

Glutaminyl-tRNA synthetase: from genetics to molecular recognition.Semantic proximity Read ↗

Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.Semantic proximity Read ↗

How mutations in tRNA distant from the anticodon affect the fidelity of decoding.Semantic proximity Read ↗

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

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