Evidence map›Paper›PMID 19523897›Full record

ArticleStructure (London, England : 1993)2009

The P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit.

Gabriel C Lander, Reza Khayat, Rui Li, Peter E Prevelige, Clinton S Potter, Bridget Carragher, John E Johnson

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

41 citing papers in PubMed, 71 citations in OpenAlex.

  1. Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024
    Review
  2. Article
  3. Review
  4. Structural insights into a spindle-shaped archaeal virus with a sevenfold symmetrical tail.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Single-particle virology.Biophysical reviews · 2020
    Review
  7. Article
  8. Time-resolved DNA release from an O-antigen-specificThe Journal of biological chemistry · 2019
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors at 2 institutions in 1 country.

Gabriel C LanderNational Resource for Automated Molecular Microscopy, The Scripps Institute, La Jolla, CA 92037, USA.
Reza Khayat
Rui Li
Peter E Prevelige
Clinton S Potter
Bridget Carragher
John E Johnson
Scripps Research Institute · USUniversity of Alabama at Birmingham · US

Funding

WORKSHOPS AND TRAININGP41RR017573 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI CARRAGHER, BRIDGET OLIVIA · 2002 to 2011
$14.2M
Studies of large and small-scale virus capsid dynamicsR01GM054076 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI JOHNSON, JOHN EMIL · 1995 to 2014
$6.2M
SUBUNIT INTERACTIONS DURING ICOSAHEDRAL CAPSID ASSEMBLYR01GM047980 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI PREVELIGE, PETER E. · 1994 to 2007
$2.0M
NCRR NIH HHS P41 RR017573NCRR NIH HHS P41 RR17573NIGMS NIH HHS R01 GM047980NIGMS NIH HHS R01 GM054076NIGMS NIH HHS R01 GM47980
6 · The paper itself

Abstract

The portal channel is a key component in the life cycle of bacteriophages and herpesviruses. The bacteriophage P22 portal is a 1 megadalton dodecameric oligomer of gp1 that plays key roles in capsid assembly, DNA packaging, assembly of the infection machinery, and DNA ejection. The portal is the nucleation site for the assembly of 39 additional subunits generated from multiple copies of four gene products (gp4, gp10, gp9, and gp26), which together form the multifunctional tail machine. These components are organized with a combination of 12-fold (gp1, gp4), 6-fold (gp10, trimers of gp9), and 3-fold (gp26, gp9) symmetry. Here we present the 3-dimensional structures of the P22 assembly-naive portal formed from expressed subunits (gp1) and the intact tail machine purified from infectious virions. The assembly-naive portal structure exhibits a striking structural similarity to the structures of the portal proteins of SPP1 and phi29 derived from X-ray crystallography.

Indexed as

VirionBacteriophage P22Binding SitesCapsid ProteinsCryoelectron MicroscopyCrystallography, X-RayModels, MolecularProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsViral Tail ProteinsCapsid Proteinsportal protein, bacteriophage P22Protein SubunitsViral Tail Proteins

Identifiers

PMID19523897
PMCPMC2714705
OpenAlexW2060788447

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.