Evidence map›Paper›PMID 22879595›Full record

ArticleThe Journal of biological chemistry2012

Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.

G Pauline Padilla-Meier, Eddie B Gilcrease, Peter R Weigele, Juliana R Cortines, Molly Siegel, Justin C Leavitt, Carolyn M Teschke, Sherwood R Casjens

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

G Pauline Padilla-MeierDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269, USA.
Eddie B Gilcrease
Peter R Weigele
Juliana R Cortines
Molly Siegel
Justin C Leavitt
Carolyn M Teschke
Sherwood R Casjens
University of Connecticut · USUniversity of Utah · US

Funding

Understanding the Protein:Protein Interactions Required for Virus AssemblyR01GM076661 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI TESCHKE, CAROLYN M · 2007 to 2022
$7.2M
DNA packaging and delivery by dsDNA virusesR01AI074825 · NIAID · UNIVERSITY OF UTAH · PI CASJENS, SHERWOOD R. · 2008 to 2012
$1.8M
NIAID NIH HHS R01 AI074825NIGMS NIH HHS R01 GM076661
6 · The paper itself

Abstract

Many viruses encode scaffolding and coat proteins that co-assemble to form procapsids, which are transient precursor structures leading to progeny virions. In bacteriophage P22, the association of scaffolding and coat proteins is mediated mainly by ionic interactions. The coat protein-binding domain of scaffolding protein is a helix turn helix structure near the C terminus with a high number of charged surface residues. Residues Arg-293 and Lys-296 are particularly important for coat protein binding. The two helices contact each other through hydrophobic side chains. In this study, substitution of the residues of the interface between the helices, and the residues in the β-turn, by aspartic acid was used examine the importance of the conformation of the domain in coat binding. These replacements strongly affected the ability of the scaffolding protein to interact with coat protein. The severity of the defect in the association of scaffolding protein to coat protein was dependent on location, with substitutions at residues in the turn and helix 2 causing the most significant effects. Substituting aspartic acid for hydrophobic interface residues dramatically perturbs the stability of the structure, but similar substitutions in the turn had much less effect on the integrity of this domain, as determined by circular dichroism. We propose that the binding of scaffolding protein to coat protein is dependent on angle of the β-turn and the orientation of the charged surface on helix 2. Surprisingly, formation of the highly complex procapsid structure depends on a relatively simple interaction.

Indexed as

Amino Acid SequenceBacteriophage P22Capsid ProteinsCircular DichroismEscherichia coliModels, MolecularMolecular ConformationMolecular Sequence DataMutagenesis, Site-DirectedMutationOligonucleotidesProphagesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryStatic ElectricityCapsid ProteinsOligonucleotides

Identifiers

PMID22879595
PMCPMC3460473
OpenAlexW2013682092

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.