Evidence map›Paper›PMID 22771211›Full record

ArticleStructure (London, England : 1993)2012

Small terminase couples viral DNA binding to genome-packaging ATPase activity.

Ankoor Roy, Anshul Bhardwaj, Pinaki Datta, Gabriel C Lander, Gino Cingolani

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
6.8field-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

49 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Structural basis for DNA recognition by a viral genome-packaging machine.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024
    Review
  8. Characterization and genomic analysis of a lyticFrontiers in microbiology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Terminase Subunits from the Pseudomonas-Phage E217.Journal of molecular biology · 2022
    Article
  15. Review
  16. Article
  17. Article
  18. Ecology, Structure, and Evolution ofAnnual review of virology · 2020
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Ankoor RoyDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA.
Anshul Bhardwaj
Pinaki Datta
Gabriel C Lander
Gino Cingolani
Thomas Jefferson University · USLawrence Berkeley National Laboratory · US

Funding

WORKSHOPS AND TRAININGP41RR017573 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI CARRAGHER, BRIDGET OLIVIA · 2002 to 2011
$14.2M
Multisubunit viral ATPases that couple ATP-hydrolysis to genome translocationR01GM100888 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI CINGOLANI, GINO · 2012 to 2020
$2.5M
Multisubunit viral ATPases that couple ATP-hydrolysis to genome translocationR56AI095974 · NIAID · THOMAS JEFFERSON UNIVERSITY · PI CINGOLANI, GINO · 2011 to 2011
$310k
NCRR NIH HHS P41 RR017573NCRR NIH HHS P41RR17573NIAID NIH HHS 1R56 AI095974-01NIAID NIH HHS R56 AI095974NIGMS NIH HHS 1R01GM100888-01A1NIGMS NIH HHS R01 GM100888
6 · The paper itself

Abstract

Packaging of viral genomes into empty procapsids is powered by a large DNA-packaging motor. In most viruses, this machine is composed of a large (L) and a small (S) terminase subunit complexed with a dodecamer of portal protein. Here we describe the 1.75 Å crystal structure of the bacteriophage P22 S-terminase in a nonameric conformation. The structure presents a central channel ∼23 Å in diameter, sufficiently large to accommodate hydrated B-DNA. The last 23 residues of S-terminase are essential for binding to DNA and assembly to L-terminase. Upon binding to its own DNA, S-terminase functions as a specific activator of L-terminase ATPase activity. The DNA-dependent stimulation of ATPase activity thus rationalizes the exclusive specificity of genome-packaging motors for viral DNA in the crowd of host DNA, ensuring fidelity of packaging and avoiding wasteful ATP hydrolysis. This posits a model for DNA-dependent activation of genome-packaging motors of general interest in virology.

Indexed as

Virus AssemblyAdenosine TriphosphateAmino Acid SequenceBacteriophage P22Binding SitesCrystallography, X-RayDNA, ViralEndodeoxyribonucleasesHydrolysisModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsAdenosine TriphosphateDNA, ViralEndodeoxyribonucleasesProtein SubunitsterminaseViral Proteins

Identifiers

PMID22771211
PMCPMC3563279
OpenAlexW2095339585

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.