Evidence map›Paper›PMID 18653535›Full record

ArticleNucleic acids research2008

Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector L-glutamine: implications of effector binding in molecular association and DNA binding.

Thirumananseri Kumarevel, Noboru Nakano, Karthe Ponnuraj, Subash C B Gopinath, Keiko Sakamoto, Akeo Shinkai, Penmetcha K R Kumar, Shigeyuki Yokoyama

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 23% of its field
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

20 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. The Lrp/AsnC-Type Regulator PA2577 Controls the EamA-like Transporter GeneInternational journal of molecular sciences · 2021
    Article
  4. Review
  5. Article
  6. Alanine dehydrogenases in mycobacteria.Journal of microbiology (Seoul, Korea) · 2019
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Host and viral transcriptional regulators in Sulfolobus: an overview.Extremophiles : life under extreme conditions · 2013
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Transcriptional activation in the context of repression mediated by archaeal histones.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

8 authors at 4 institutions in 2 countries.

Thirumananseri KumarevelRIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan. tskvel@spring8.or.jp
Noboru Nakano
Karthe Ponnuraj
Subash C B Gopinath
Keiko Sakamoto
Akeo Shinkai
Penmetcha K R Kumar
Shigeyuki Yokoyama
SPring-8 · JPThe University of Tokyo · JPNational Institute of Advanced Industrial Science and Technology · JPUniversity of Madras · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genome analyses have revealed that members of the Lrp/AsnC family of transcriptional regulators are widely distributed among prokaryotes, including both bacteria and archaea. These regulatory proteins are involved in cellular metabolism in both global and specific manners, depending on the availability of the exogenous amino acid effectors. Here we report the first crystal structure of glutamine receptor protein (Grp) from Sulfolobus tokodaii strain 7, in the ligand-free and glutamine-bound (Grp-Gln) forms. Although the overall structures of both molecules are similar, a significant conformational change was observed at the ligand [L-glutamine (Gln)] binding site in the effector domain, which may be essential for further stabilization of the octameric structure, and in turn for facilitating DNA binding. In addition, we predicted promoter for the grp gene, and these analyses suggested the importance of cooperative binding to the protein. To gain insights into the ligand-induced conformational changes, we mutated all of the ligand-binding residues in Grp, and revealed the importance of Gln binding by biochemical and structural analyses. Further structural analyses showed that Y77 is crucial for ligand binding, and that the residues T132 and T134, which are highly conserved among the Lrp family of proteins, fluctuates between the active and inactive conformations, thus affecting protein oligomerization for DNA binding.

Indexed as

SulfolobusAmino Acid SequenceArchaeal ProteinsBinding SitesCrystallographyDNADNA-Binding ProteinsGlutamineModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPromoter Regions, GeneticProtein BindingProtein ConformationProtein Structure, TertiaryTranscription FactorsArchaeal ProteinsDNADNA-Binding ProteinsGlutamineTranscription Factors

Identifiers

PMID18653535
PMCPMC2504300
OpenAlexW2123222426

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LicenceCC BY-NC
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.