Evidence map›Paper›PMID 37769963›Full record

ArticleJournal of molecular biology2023

Evolutionary Engineering a Larger Porin Using a Loop-to-Hairpin Mechanism.

Rik Dhar, Alexander M Bowman, Brunojoel Hatungimana, Joanna Sg Slusky

Abstract read
In one paragraph

Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Rik DharDepartment of Molecular Biosciences, The University of Kansas, Lawrence, KS 66045, USA. Electronic address: https://twitter.com/Rik_Skywalker.
Alexander M BowmanDepartment of Molecular Biosciences, The University of Kansas, Lawrence, KS 66045, USA.
Brunojoel HatungimanaDepartment of Molecular Biosciences, The University of Kansas, Lawrence, KS 66045, USA.
Joanna Sg SluskyDepartment of Molecular Biosciences, The University of Kansas, Lawrence, KS 66045, USA; Computational Biology Program, The University of Kansas, Lawrence, KS 66047, USA. Electronic address: slusky@ku.edu.

Funding

Mentoring CoreP20GM103418 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI Douglas E Wright · 2012 to 2026
$63.0M
Synthetic Chemical Biology CoreP20GM113117 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI OROZCO, ROBIN C. · 2016 to 2025
$23.9M
DESIGNED BETA-STRANDS FOR INHIBITING EFFLUX PUMPS AND DISABLING ANTIBIOTIC RESISTANCEDP2GM128201 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI SLUSKY, JOANNA SG · 2017 to 2017
$2.3M
Plugging & Pulling-in: tuning peptides for TolC to overcome antibiotic resistanceR01GM148583 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI Joanna SG Slusky · 2023 to 2026
$1.3M
NIGMS NIH HHS DP2 GM128201NIGMS NIH HHS P20 GM103418NIGMS NIH HHS P20 GM113117NIGMS NIH HHS R01 GM148583
6 · The paper itself

Abstract

In protein evolution, diversification is generally driven by genetic duplication. The hallmarks of this mechanism are visible in the repeating topology of various proteins. In outer membrane β-barrels, duplication is visible with β-hairpins as the repeating unit of the barrel. In contrast to the overall use of duplication in diversification, a computational study hypothesized evolutionary mechanisms other than hairpin duplications leading to increases in the number of strands in outer membrane β-barrels. Specifically, the topology of some 16- and 18-stranded β-barrels appear to have evolved through a loop to β-hairpin transition. Here we test this novel evolutionary mechanism by creating a chimeric protein from an 18-stranded β-barrel and an evolutionarily related 16-stranded β-barrel. The chimeric combination of the two was created by replacing loop L3 of the 16-stranded barrel with the sequentially matched transmembrane β-hairpin region of the 18-stranded barrel. We find the resulting chimeric protein is stable and has characteristics of increased strand number. This study provides the first experimental evidence supporting the evolution through a loop to β-hairpin transition.

Indexed as

Bacterial Outer Membrane ProteinsPorinsBacterial ProteinsDirected Molecular EvolutionProtein Conformation, beta-StrandProtein DomainsProtein FoldingRecombinant Fusion ProteinsBacterial Outer Membrane ProteinsBacterial Proteinsmajor outer membrane protein, Campylobacter jejuniporin protein, NeisseriaPorinsRecombinant Fusion Proteinsloop-to-hairpinmolecular evolutionneisserial porinouter membrane proteinsβ-barrel

Identifiers

PMID37769963
PMCPMC11215794

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Registered trials

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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.