Evidence map›Paper›PMID 14671330›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains.

Xiang-Lei Yang, Francella J Otero, Robert J Skene, Duncan E McRee, Paul Schimmel, Llúis Ribas de Pouplana

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed.

  1. Article
  2. Thermal Titration Molecular Dynamics: The Revenge of the Fragments.Journal of chemical information and modeling · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Enzyme catalysis prior to aromatic residues: Reverse engineering of a dephospho-CoA kinase.Protein science : a publication of the Protein Society · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Modern diversification of the amino acid repertoire driven by oxygen.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Bioinformatic Analysis Reveals Archaeal tRNALife (Basel, Switzerland) · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Xiang-Lei YangDepartments of Molecular Biology and Chemistry, The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Francella J Otero
Robert J Skene
Duncan E McRee
Paul Schimmel
Llúis Ribas de Pouplana

Funding

INVESTIGATIONS OF REACTIONS OF PHYSIOLOGICAL IMPORTANCER01GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2011
$6.6M
REACTIONS OF PHYSIOLOGICAL IMPORTANCER37GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI SCHIMMEL, PAUL R · 1989 to 1998
–
NIGMS NIH HHS GM15539NIGMS NIH HHS R01 GM015539
6 · The paper itself

Abstract

Early forms of the genetic code likely generated "statistical" proteins, with similar side chains occupying the same sequence positions at different ratios. In this scenario, groups of related side chains were treated by aminoacyl-tRNA synthetases as a single molecular species until a discrimination mechanism developed that could separate them. The aromatic amino acids tryptophan, tyrosine, and phenylalanine likely constituted one of these groups. A crystal structure of human tryptophanyl-tRNA synthetase was solved at 2.1 A with a tryptophanyl-adenylate bound at the active site. A cocrystal structure of an active fragment of human tyrosyl-tRNA synthetase with its cognate amino acid analog was also solved at 1.6 A. The two structures enabled active site identifications and provided the information for structure-based sequence alignments of approximately 45 orthologs of each enzyme. Two critical positions shared by all tyrosyl-tRNA synthetases and tryptophanyl-tRNA synthetases for amino acid discrimination were identified. The variations at these two positions and phylogenetic analyses based on the structural information suggest that, in contrast to many other amino acids, discrimination of tyrosine from tryptophan occurred late in the development of the genetic code.

Indexed as

Genetic CodeAdenosine MonophosphateAmino Acid SequenceBinding SitesConserved SequenceCrystallography, X-RayGeobacillus stearothermophilusHumansModels, MolecularMolecular Sequence DataPhylogenyProtein ConformationSensitivity and SpecificitySequence AlignmentSequence Homology, Amino AcidTryptophanAdenosine MonophosphateTryptophanTryptophan-tRNA Ligase

Identifiers

PMID14671330
PMCPMC307575

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.