Evidence map›Paper›PMID 27667692›Full record

ArticleStructure (London, England : 1993)2016

Common Evolutionary Origin of Procapsid Proteases, Phage Tail Tubes, and Tubes of Bacterial Type VI Secretion Systems.

Andrei Fokine, Michael G Rossmann

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Phenotypic characterization and genomic analysis ofCurrent research in food science · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Bacteriophage ICP1: A Persistent Predator ofAnnual review of virology · 2021
    Article
  12. International journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Genes · 2019
    Article
  19. Global Proteomic Profiling ofJournal of virology · 2019
    Article
  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

2 authors at 1 institution in 1 country.

Andrei FokineDepartment of Biological Sciences, Hockmeyer Hall of Structural Biology, Purdue University, 240 South Martin Jischke Drive, West Lafayette, IN 47907, USA. Electronic address: afokine@purdue.edu.
Michael G RossmannDepartment of Biological Sciences, Hockmeyer Hall of Structural Biology, Purdue University, 240 South Martin Jischke Drive, West Lafayette, IN 47907, USA. Electronic address: mr@purdue.edu.
Purdue University West Lafayette · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
Structural studies of bacteriophage T4 and their potential medical applicationsR01AI081726 · NIAID · PURDUE UNIVERSITY · PI KUHN, RICHARD J., RAO, VENIGALLA B. · 2010 to 2019
$6.2M
Structural studies of bacteriophage T4 and their potential medical applicationsR56AI081726 · NIAID · PURDUE UNIVERSITY · PI ROSSMANN, MICHAEL G · 2009 to 2009
$600k
NCI NIH HHS P30 CA023168NIAID NIH HHS R01 AI081726NIAID NIH HHS R56 AI081726
6 · The paper itself

Abstract

Many large viruses, including tailed dsDNA bacteriophages and herpesviruses, assemble their capsids via formation of precursors, called procapsids or proheads. The prohead has an internal core, made of scaffolding proteins, and an outer shell, formed by the major capsid protein. The prohead usually contains a protease, which is activated during capsid maturation to destroy the inner core and liberate space for the genome. Here, we report a 2.0 Å resolution structure of the pentameric procapsid protease of bacteriophage T4, gene product (gp)21. The structure corresponds to the enzyme's pre-active state in which its N-terminal region blocks the catalytic center, demonstrating that the activation mechanism involves self-cleavage of nine N-terminal residues. We describe similarities and differences between T4 gp21 and related herpesvirus proteases. We found that gp21 and the herpesvirus proteases have similarity with proteins forming the tubes of phage tails and bacterial type VI secretion systems, suggesting their common evolutionary origin.

Indexed as

Amino Acid MotifsBacteriophage T4CapsidCatalytic DomainEndopeptidasesEvolution, MolecularHerpesviridaeModels, MolecularProtein FoldingType VI Secretion SystemsViral ProteinsEndopeptidasesgp21 morphogenetic proteinase, phage T4Type VI Secretion SystemsViral Proteinsbacterial type VI secretion systembacteriophageherpesvirusphage tail tubeprocapsidprohead proteaseself-cleavagevirus assembly

Identifiers

PMID27667692
PMCPMC5093050
OpenAlexW2521762172

What OpenQuestion holds

Textmetadata
LicenceTDM
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.