Evidence map›Paper›PMID 23884409›Full record

ArticleThe Journal of biological chemistry2013

Structural characterization of the bacteriophage T7 tail machinery.

Ana Cuervo, Mar Pulido-Cid, Mónica Chagoyen, Rocío Arranz, Verónica A González-García, Carmela Garcia-Doval, José R Castón, José M Valpuesta, Mark J van Raaij, Jaime Martín-Benito and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Cryo-EM structure of cyanopodophage A4 reveals a pentameric pre-ejectosome in the double-stabilized capsid.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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

11 authors at 2 institutions in 1 country.

Ana CuervoFrom the Structure of Macromolecules and.
Mar Pulido-CidFrom the Structure of Macromolecules and.
Mónica ChagoyenSystems Biology Departments, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Darwin 3 and.
Rocío ArranzFrom the Structure of Macromolecules and.
Verónica A González-GarcíaFrom the Structure of Macromolecules and.
Carmela Garcia-DovalFrom the Structure of Macromolecules and.
José R CastónFrom the Structure of Macromolecules and.
José M ValpuestaFrom the Structure of Macromolecules and.
Mark J van RaaijFrom the Structure of Macromolecules and.
Jaime Martín-BenitoFrom the Structure of Macromolecules and.
José L CarrascosaFrom the Structure of Macromolecules and; the Instituto Madrileño de Estudios Avanzados en Nanociencia, Cantoblanco, 28049 Madrid, Spain. Electronic address: jlcarras@cnb.csic.es.
Consejo Superior de Investigaciones Científicas · ESMadrid Institute for Advanced Studies · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most bacterial viruses need a specialized machinery, called "tail," to inject their genomes inside the bacterial cytoplasm without disrupting the cellular integrity. Bacteriophage T7 is a well characterized member of the Podoviridae family infecting Escherichia coli, and it has a short noncontractile tail that assembles sequentially on the viral head after DNA packaging. The T7 tail is a complex of around 2.7 MDa composed of at least four proteins as follows: the connector (gene product 8, gp8), the tail tubular proteins gp11 and gp12, and the fibers (gp17). Using cryo-electron microscopy and single particle image reconstruction techniques, we have determined the precise topology of the tail proteins by comparing the structure of the T7 tail extracted from viruses and a complex formed by recombinant gp8, gp11, and gp12 proteins. Furthermore, the order of assembly of the structural components within the complex was deduced from interaction assays with cloned and purified tail proteins. The existence of common folds among similar tail proteins allowed us to obtain pseudo-atomic threaded models of gp8 (connector) and gp11 (gatekeeper) proteins, which were docked into the corresponding cryo-EM volumes of the tail complex. This pseudo-atomic model of the connector-gatekeeper interaction revealed the existence of a common molecular architecture among viruses belonging to the three tailed bacteriophage families, strongly suggesting that a common molecular mechanism has been favored during evolution to coordinate the transition between DNA packaging and tail assembly.

Indexed as

Bacteriophage T7Cryoelectron MicroscopyDNA, ViralEscherichia coliMultiprotein ComplexesViral Proteinsbacteriophage T7 leg protein gp17DNA, ViralMultiprotein ComplexesViral ProteinsBacteriophageDNA VirusesElectron Microscopy (EM)Protein StructureVirus AssemblyVirus Structure

Identifiers

PMID23884409
PMCPMC3764833
OpenAlexW2089040869

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.