Evidence map›Paper›PMID 23570450›Full record

ArticleBiochemistry2013

A circularly permuted photoactive yellow protein as a scaffold for photoswitch design.

Anil Kumar, Darcy C Burns, M Sameer Al-Abdul-Wahid, G Andrew Woolley

Abstract read
In one paragraph

Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Structure-based design of a photoswitchable affibody scaffold.Protein science : a publication of the Protein Society · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Optimizing optogenetic constructs for control over signaling and cell behaviours.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2015
    Review
  9. Article
  10. Article
  11. 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 1 country.

Anil KumarDepartment of Chemistry, University of Toronto , 80 St. George Street, Toronto, ON M5S 3H6, Canada.
Darcy C Burns
M Sameer Al-Abdul-Wahid
G Andrew Woolley
University of Toronto · CAMcGill University · CA

Funding

Photo-chemical tools for manipulating neural plasticityR01MH086379 · NIMH · UNIVERSITY OF TORONTO · PI WOOLLEY, ANDREW · 2009 to 2012
$667k
CIHRNIMH NIH HHS R01 MH086379
6 · The paper itself

Abstract

Upon blue light irradiation, photoactive yellow protein (PYP) undergoes a conformational change that involves large movements at the N-terminus of the protein. We reasoned that this conformational change might be used to control other protein or peptide sequences if these were introduced as linkers connecting the N- and C-termini of PYP in a circular permutant. For such a design strategy to succeed, the circularly permuted PYP (cPYP) would have to fold normally and undergo a photocycle similar to that of the wild-type protein. We created a test cPYP by connecting the N- and C-termini of wild-type PYP (wtPYP) with a GGSGGSGG linker polypeptide and introducing new N- and C-termini at G115 and S114, respectively. Biophysical analysis indicated that this cPYP adopts a dark-state conformation much like wtPYP and undergoes wtPYP-like photoisomerization driven by blue light. However, thermal recovery of dark-state cPYP is ∼10-fold faster than that of wtPYP, so that very bright light is required to significantly populate the light state. Targeted mutations at M121E (M100 in wtPYP numbering) were found to enhance the light sensitivity substantially by lengthening the lifetime of the light state to ∼10 min. Nuclear magnetic resonance (NMR), circular dichroism, and UV-vis analysis indicated that the M121E-cPYP mutant also adopts a dark-state structure like that of wtPYP, although protonated and deprotonated forms of the chromophore coexist, giving rise to a shoulder near 380 nm in the UV-vis absorption spectrum. Fluorine NMR studies with fluorotryptophan-labeled M121E-cPYP show that blue light drives large changes in conformational dynamics and leads to solvent exposure of Trp7 (Trp119 in wtPYP numbering), consistent with substantial rearrangement of the N-terminal cap structure. M121E-cPYP thus provides a scaffold that may allow a wider range of photoswitchable protein designs via replacement of the linker polypeptide with a target protein or peptide sequence.

Indexed as

Bacterial ProteinsBiophysical PhenomenaCircular DichroismModels, MolecularMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhotochemical ProcessesPhotoreceptors, MicrobialProtein ConformationProtein EngineeringSpectrophotometryBacterial Proteinsphotoactive yellow protein, BacteriaPhotoreceptors, Microbial

Identifiers

PMID23570450
PMCPMC3795922
OpenAlexW2006359840

What OpenQuestion holds

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LicenceTDM
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.