Evidence map›Paper›PMID 19164760›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

The nature of the TRAP-Anti-TRAP complex.

Masahiro Watanabe, Jonathan G Heddle, Kenichi Kikuchi, Satoru Unzai, Satoko Akashi, Sam-Yong Park, Jeremy R H Tame

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 33 citations in OpenAlex.

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  13. Resurrecting the Dead (Molecules).Computational and structural biotechnology journal · 2017
    Review
  14. Computational design of a self-assembling symmetrical β-propeller protein.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
  16. Gene regulation by substoichiometric heterocomplex formation of undecameric TRAP and trimeric anti-TRAP.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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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

7 authors at 2 institutions in 2 countries.

Masahiro WatanabeYokohama City University, Tsurumi, Suehiro 1-7-29, Yokohama 230-0045, Japan.
Jonathan G Heddle
Kenichi Kikuchi
Satoru Unzai
Satoko Akashi
Sam-Yong Park
Jeremy R H Tame
Yokohama City University · JPSequenom (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tryptophan biosynthesis is subject to exquisite control in species of Bacillus and has become one of the best-studied model systems in gene regulation. The protein TRAP (trp RNA-binding attenuation protein) predominantly forms a ring-shaped 11-mer, which binds cognate RNA in the presence of tryptophan to suppress expression of the trp operon. TRAP is itself regulated by the protein Anti-TRAP, which binds to TRAP and prevents RNA binding. To date, the nature of this interaction has proved elusive. Here, we describe mass spectrometry and analytical centrifugation studies of the complex, and 2 crystal structures of the TRAP-Anti-TRAP complex. These crystal structures, both refined to 3.2-A resolution, show that Anti-TRAP binds to TRAP as a trimer, sterically blocking RNA binding. Mass spectrometry shows that 11-mer TRAP may bind up to 5 AT trimers, and an artificial 12-mer TRAP may bind 6. Both forms of TRAP make the same interactions with Anti-TRAP. Crystallization of wild-type TRAP with Anti-TRAP selectively pulls the 12-mer TRAP form out of solution, so the crystal structure of wild-type TRAP-Anti-TRAP complex reflects a minor species from a mixed population.

Indexed as

BacillusBacterial ProteinsBinding SitesCrystallography, X-RayGene Expression Regulation, BacterialHydrogen BondingMass SpectrometryModels, BiologicalModels, MolecularMolecular ConformationProtein BindingProtein ConformationRNA-Binding ProteinsSolventsSpectrometry, Mass, Electrospray IonizationTranscription FactorsBacterial ProteinsMtrB protein, BacteriaRNA-Binding ProteinsSolventsTranscription FactorsTryptophan

Identifiers

PMID19164760
PMCPMC2650128
OpenAlexW2098274928

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.