Evidence map›Paper›PMID 25587134›Full record

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

The NMR-Rosetta capsid model of M13 bacteriophage reveals a quadrupled hydrophobic packing epitope.

Omry Morag, Nikolaos G Sgourakis, David Baker, Amir Goldbourt

Open access · bronzeAbstract 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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
14.7field-weighted citation impact, top 1% 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

37 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Role of Phage Capsid in the Resistance to UV-C Radiations.International journal of molecular sciences · 2021
    Article
  13. Review
  14. Article
  15. Article
  16. Virus lasers for biological detection.Nature communications · 2019
    Article
  17. Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Review
  19. Article
  20. Cryo-electron microscopy structure of the filamentous bacteriophage IKe.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

4 authors at 2 institutions in 2 countries.

Omry MoragSchool of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Ramat Aviv 69978, Tel Aviv, Israel; and.
Nikolaos G SgourakisDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA 98195.
Amir GoldbourtSchool of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Ramat Aviv 69978, Tel Aviv, Israel; and amirgo@post.tau.ac.il.
Tel Aviv University · ILUniversity of Washington · US

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

Filamentous phage are elongated semiflexible ssDNA viruses that infect bacteria. The M13 phage, belonging to the family inoviridae, has a length of ∼1 μm and a diameter of ∼7 nm. Here we present a structural model for the capsid of intact M13 bacteriophage using Rosetta model building guided by structure restraints obtained from magic-angle spinning solid-state NMR experimental data. The C5 subunit symmetry observed in fiber diffraction studies was enforced during model building. The structure consists of stacked pentamers with largely alpha helical subunits containing an N-terminal type II β-turn; there is a rise of 16.6-16.7 Å and a tilt of 36.1-36.6° between consecutive pentamers. The packing of the subunits is stabilized by a repeating hydrophobic stacking pocket; each subunit participates in four pockets by contributing different hydrophobic residues, which are spread along the subunit sequence. Our study provides, to our knowledge, the first magic-angle spinning NMR structure of an intact filamentous virus capsid and further demonstrates the strength of this technique as a method of choice to study noncrystalline, high-molecular-weight molecular assemblies.

Indexed as

Models, MolecularNuclear Magnetic Resonance, BiomolecularBacteriophage M13CapsidProtein Structure, Secondaryfilamentous bacteriophagemagic-angle spinningRosetta modelingsolid-state NMRstructure determination

Identifiers

PMID25587134
PMCPMC4313819
OpenAlexW2166280704

What OpenQuestion holds

Textmetadata
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.