Evidence map›Paper›PMID 26882199›Full record

ArticlePloS one2016

Structure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel.

Haiyan Zhao, Jeffrey A Speir, Tsutomu Matsui, Zihan Lin, Lingfei Liang, Anna Y Lynn, Brittany Varnado, Thomas M Weiss, Liang Tang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

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  9. Ecology, Structure, and Evolution ofAnnual review of virology · 2020
    Review
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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

9 authors at 4 institutions in 1 country.

Haiyan ZhaoDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, Kansas, United States of America.
Jeffrey A SpeirNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, California, United States of America.
Tsutomu MatsuiStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, 14 2575 Sand Hill Road, MS69, Menlo Park, California, United States of America.
Zihan LinDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, Kansas, United States of America.
Lingfei LiangDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, Kansas, United States of America.
Anna Y LynnDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, Kansas, United States of America.
Brittany VarnadoDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, Kansas, United States of America.
Thomas M WeissStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, 14 2575 Sand Hill Road, MS69, Menlo Park, California, United States of America.
Liang TangDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, Kansas, United States of America.
University of Kansas · USScripps Research Institute · USStanford Synchrotron Radiation Lightsource · USStanford University · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Genome packaging in DNA virusesR01GM090010 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI TANG, LIANG · 2010 to 2014
$1.3M
NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41GM103310NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM090010NIGMS NIH HHS R01GM090010
6 · The paper itself

Abstract

The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in vitro. The electron microscopic structure of the gp12 assembly shows a ~150-Å, mushroom-like architecture consisting of a crown domain and a tube-like domain, which embraces a 25-Å-wide channel that could precisely accommodate dsDNA. The constricted channel suggests that gp12 mediates rapid, uni-directional injection of phage DNA into host cells by providing a molecular conduit for DNA translocation. The assembly exhibits a 10-fold symmetry, which may be a common feature among DNA-injection proteins of P22-like phages and may suggest a symmetry mismatch with respect to the 6-fold symmetric phage tail. The gp12 monomer is highly flexible in solution, supporting a mechanism for translocation of the protein through the conduit of the phage tail toward the host cell envelope, where it assembles into a DNA-injection device.

Indexed as

Models, MolecularProtein MultimerizationBacteriophagesDNA, ViralImaging, Three-DimensionalProtein Structure, TertiarySolutionsViral ProteinsDNA, ViralSolutionsViral Proteins

Identifiers

PMID26882199
PMCPMC4755594
OpenAlexW2278308361

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.