Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins.

doi:10.1006/jmbi.1993.1353

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

Back to search

Article

Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins.

Journal of molecular biology - 20 Jun 1993

Fourmy D, Dardel F, Blanquet S

Abstract excerpt

Methionyl-tRNA synthetase from Escherichia coli contains one tightly bound zinc atom per subunit. The region encompassing residues 138 to 163 of this enzyme is responsible for the metal binding. A 28-mer peptide corresponding to these residues was expressed in vivo and shown to contain approximat...

Topics

Amino Acid Sequence
Cysteine
Escherichia coli
Gene Products, gag
Magnetic Resonance Spectroscopy
Methionine-tRNA Ligase
Models, Molecular
Molecular Sequence Data
Mutation
Peptide Fragments
Protein Conformation
Protein Precursors
Rubredoxins
Sequence Homology, Amino Acid
Zinc

Source

Open in PubMed

Identifiers

PMID: 8515466
DOI: 10.1006/jmbi.1993.1353

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8515466-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics