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

The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRS(apm)) is a monomer in solution.

FEBS letters - 18 Mar 2013

Choudhury Aparajita, Banerjee Rajat

Abstract excerpt

Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRSapm) was the first reported aminoacyl-tRNA synthetase of viral origin. The previous crystal structure of TyrRSapm showed a non-canonical orientation of the dimer conformation and the CP1 domain, responsible for dimer formation, displays a major modification of a motif structurally conserved in other TyrRS structures. An earlier study reported that...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Diphosphates
Share to Disulfides

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

Share to Protein Multimerization

Share to Solutions

Share to Thermodynamics

Share to Tyrosine-tRNA Ligase

Share to Ultracentrifugation

Source

Identifiers

PMID: 23384724
DOI: 10.1016/j.febslet.2013.01.048

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

The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRS(apm)) is a monomer in solution.PMID 23384724Read ↗

Discrimination between transfer-RNAs by tyrosyl-tRNA synthetase.Semantic proximity Read ↗

Structural insights into dynamics of the BMV TLS aminoacylationSemantic proximity Read ↗

Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase.Semantic proximity Read ↗

Improved Incorporation of Noncanonical Amino Acids by an Engineered tRNA(Tyr) Suppressor.Semantic proximity Read ↗

Non-canonical substrates of aminoacyl-tRNA synthetases: the tRNA-like structure of brome mosaic virus genomic RNA.Semantic proximity Read ↗

A model of synthetase/transfer RNA interaction as deduced by protein engineering.Semantic proximity Read ↗

Mutational separation of aminoacylation and cytokine activities of human tyrosyl-tRNA synthetase.Semantic proximity Read ↗

A simple system for expression of proteins containing 3-azidotyrosine at a pre-determined site in Escherichia coli.Semantic proximity Read ↗

Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase.Semantic proximity Read ↗

Correlating amino acid conservation with function in tyrosyl-tRNA synthetase.Semantic proximity Read ↗

Altered oligomerization properties of N316 mutants of Escherichia coli TyrR.Semantic proximity Read ↗

The importance of charge in perturbing the aromatic glue stabilizing the protein-protein interface of homodimeric tRNA-guanine transglycosylaseSemantic proximity Read ↗

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