Evidence map›Paper›PMID 26150523›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structure and mechanism of the ATPase that powers viral genome packaging.

Brendan J Hilbert, Janelle A Hayes, Nicholas P Stone, Caroline M Duffy, Banumathi Sankaran, Brian A Kelch

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Terminase Subunits from the Pseudomonas-Phage E217.Journal of molecular biology · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Viral packaging ATPases utilize a glutamate switch to couple ATPase activity and DNA translocation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

6 authors.

Brendan J HilbertDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605;
Janelle A HayesDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605;
Nicholas P StoneDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605;
Caroline M DuffyDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605;
Banumathi SankaranBerkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Brian A KelchDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605; brian.kelch@umassmed.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many viruses package their genomes into procapsids using an ATPase machine that is among the most powerful known biological motors. However, how this motor couples ATP hydrolysis to DNA translocation is still unknown. Here, we introduce a model system with unique properties for studying motor structure and mechanism. We describe crystal structures of the packaging motor ATPase domain that exhibit nucleotide-dependent conformational changes involving a large rotation of an entire subdomain. We also identify the arginine finger residue that catalyzes ATP hydrolysis in a neighboring motor subunit, illustrating that previous models for motor structure need revision. Our findings allow us to derive a structural model for the motor ring, which we validate using small-angle X-ray scattering and comparisons with previously published data. We illustrate the model's predictive power by identifying the motor's DNA-binding and assembly motifs. Finally, we integrate our results to propose a mechanistic model for DNA translocation by this molecular machine.

Indexed as

DNA PackagingGenome, ViralVirus AssemblyAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceArginineBacteriophagesBiophysical PhenomenaElectrophoresis, Polyacrylamide GelModels, BiologicalModels, MolecularMolecular Sequence DataProtein Structure, TertiaryReproducibility of ResultsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateArginineViral ProteinsASCE ATPasebacteriophagemotor proteinthermophiletranslocase

Identifiers

PMID26150523
PMCPMC4517215

What OpenQuestion holds

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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.