Evidence map›Paper›PMID 19835886›Full record

ArticleJournal of molecular biology2010

Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages.

Li Qin, Andrei Fokine, Erin O'Donnell, Venigalla B Rao, Michael G Rossmann

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.8field-weighted citation impact, top 6% 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

63 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Templated trimerization of the phage L decoration protein on capsids.Protein science : a publication of the Protein Society · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Capsid Structure ofJournal of virology · 2021
    Article
  18. Engineering T4 Bacteriophage forACS synthetic biology · 2021
    Article
  19. Article
  20. Article

3 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

5 authors at 2 institutions in 1 country.

Li QinDepartment of Biology, The Catholic University of America, 620 Michigan Avenue NE, Washington, DC 20064, USA.
Andrei Fokine
Erin O'Donnell
Venigalla B Rao
Michael G Rossmann
Catholic University of America · USState Street (United States) · US

Funding

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
Phase T4 Head Assembly and Initiation of InfectionR01AI011676 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI BLACK, LINDSAY W · 1985 to 2013
$4.1M
A Multicomponent Anthrax Vaccine using Phage T4 DisplayU01AI056443 · NIAID · CATHOLIC UNIVERSITY OF AMERICA · PI RAO, VENIGALLA B. · 2003 to 2007
$3.3M
STRUCTURE OF A SMALL SPHERICAL VIRUSR01AI011219 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 1985 to 2020
$2.4M
Multivalent Plague, Anthrax Vaccines Using Bacteriophage T4 DisplayU01AI082086 · NIAID · CATHOLIC UNIVERSITY OF AMERICA · PI RAO, VENIGALLA B. · 2009 to 2013
$2.2M
Structural studies of bacteriophage T4 and their potential medical applicationsR56AI081726 · NIAID · PURDUE UNIVERSITY · PI ROSSMANN, MICHAEL G · 2009 to 2009
$600k
NIAID NIH HHS AI056443NIAID NIH HHS R01 AI011219NIAID NIH HHS R01 AI011676NIAID NIH HHS R01 AI081726NIAID NIH HHS R56 AI081726NIAID NIH HHS R56AI081726NIAID NIH HHS U01 AI056443NIAID NIH HHS U01 AI082086
6 · The paper itself

Abstract

Many viruses need to stabilize their capsid structure against DNA pressure and for survival in hostile environments. The 9-kDa outer capsid protein (Soc) of bacteriophage T4, which stabilizes the virus, attaches to the capsid during the final stage of maturation. There are 870 Soc molecules that act as a "glue" between neighboring hexameric capsomers, forming a "cage" that stabilizes the T4 capsid against extremes of pH and temperature. Here we report a 1.9 A resolution crystal structure of Soc from the bacteriophage RB69, a close relative of T4. The RB69 crystal structure and a homology model of T4 Soc were fitted into the cryoelectron microscopy reconstruction of the T4 capsid. This established the region of Soc that interacts with the major capsid protein and suggested a mechanism, verified by extensive mutational and biochemical studies, for stabilization of the capsid in which the Soc trimers act as clamps between neighboring capsomers. The results demonstrate the factors involved in stabilizing not only the capsids of T4-like bacteriophages but also many other virus capsids.

Indexed as

Amino Acid SequenceBacteriophage T4Binding SitesCapsid ProteinsCryoelectron MicroscopyCrystallography, X-RayEvolution, MolecularModels, MolecularMolecular Sequence DataMutationProtein MultimerizationProtein StabilityProtein Structure, QuaternaryRecombinant ProteinsSequence Homology, Amino AcidVirus AssemblyCapsid ProteinsRecombinant Proteinssmall outer capsid protein, bacteriophage T4

Identifiers

PMID19835886
PMCPMC2813359
OpenAlexW1974221260

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.