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

Amino acid binding by the class I aminoacyl-tRNA synthetases: role for a conserved proline in the signature sequence.

Protein science : a publication of the Protein Society - 1 May 1992

Burbaum J J, Schimmel P

Abstract excerpt

Although partial or complete three-dimensional structures are known for three Class I aminoacyl-tRNA synthetases, the amino acid-binding sites in these proteins remain poorly characterized. To explore the methionine binding site of Escherichia coli methionyl-tRNA synthetase, we chose to study a specific, randomly generated methionine auxotroph that contains a mutant methionyl-tRNA synthetase whose defect is...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cloning, Molecular
Share to Escherichia coli

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

Share to Kinetics

Share to Molecular Sequence Data

Share to Phenotype

Share to Polymerase Chain Reaction

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 1304356
DOI: 10.1002/pro.5560010503
PMCID: PMC2142228

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

Amino acid binding by the class I aminoacyl-tRNA synthetases: role for a conserved proline in the signature sequence.PMID 1304356Read ↗

An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing.Semantic proximity Read ↗

Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP.Semantic proximity Read ↗

The invariant arginine in motif 2 of Escherichia coli alanyl-tRNA synthetase is important for catalysis but not for substrate binding.Semantic proximity Read ↗

Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations.Semantic proximity Read ↗

Backbone Brackets and Arginine Tweezers delineate Class I and Class II aminoacyl tRNA synthetases.Semantic proximity Read ↗

tRNA leucine identity and recognition sets.Semantic proximity Read ↗

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

Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway.Semantic proximity Read ↗

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

Evidence for distinct locations for metal binding sites in two closely related class I tRNA synthetases.Semantic proximity Read ↗

Synonymous lysine codon usage modification in a mobile antibiotic resistance gene similarly alters protein production in bacterial species with divergent lysine codon usage biases because it removes a duplicate AAA lysine codonSemantic proximity Read ↗

Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases.Semantic proximity Read ↗

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