Evidence map›Paper›PMID 25923520›Full record

ArticlePloS one2015

X-Ray Crystal Structure and Properties of Phanta, a Weakly Fluorescent Photochromic GFP-Like Protein.

Craig Don Paul, Daouda A K Traore, Seth Olsen, Rodney J Devenish, Devin W Close, Toby D M Bell, Andrew Bradbury, Matthew C J Wilce, Mark Prescott

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2015. 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

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.

Craig Don PaulDepartment of Neuro- and Sensory Physiology, University Medicine, Göttingen, 37073, Göttingen, Germany.
Daouda A K TraoreDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton campus, Victoria, 3800, Australia.
Seth OlsenSchool of Mathematics and Physics, The University of Queensland, Brisbane, Queensland, 4072, Australia.
Rodney J DevenishDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton campus, Victoria, 3800, Australia.
Devin W CloseBioscience Division, Los Alamos National Laboratory, Los Alamos, NM, 87545, United States of America.
Toby D M BellSchool of Chemistry, Monash University, Clayton campus, Victoria, 3800, Australia.
Andrew BradburyBioscience Division, Los Alamos National Laboratory, Los Alamos, NM, 87545, United States of America.
Matthew C J WilceDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton campus, Victoria, 3800, Australia.
Mark PrescottDepartment of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton campus, Victoria, 3800, Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phanta is a reversibly photoswitching chromoprotein (ΦF, 0.003), useful for pcFRET, that was isolated from a mutagenesis screen of the bright green fluorescent eCGP123 (ΦF, 0.8). We have investigated the contribution of substitutions at positions His193, Thr69 and Gln62, individually and in combination, to the optical properties of Phanta. Single amino acid substitutions at position 193 resulted in proteins with very low ΦF, indicating the importance of this position in controlling the fluorescence efficiency of the variant proteins. The substitution Thr69Val in Phanta was important for supressing the formation of a protonated chromophore species observed in some His193 substituted variants, whereas the substitution Gln62Met did not significantly contribute to the useful optical properties of Phanta. X-ray crystal structures for Phanta (2.3 Å), eCGP123T69V (2.0 Å) and eCGP123H193Q (2.2 Å) in their non-photoswitched state were determined, revealing the presence of a cis-coplanar chromophore. We conclude that changes in the hydrogen-bonding network supporting the cis-chromophore, and its contacts with the surrounding protein matrix, are responsible for the low fluorescence emission of eCGP123 variants containing a His193 substitution.

Indexed as

Amino Acid SubstitutionCrystallography, X-RayEscherichia coliFluorescenceFluorescent DyesGreen Fluorescent ProteinsHydrogen BondingModels, MolecularPhotochemical ProcessesProtein ConformationFluorescent DyesGreen Fluorescent Proteins

Identifiers

PMID25923520
PMCPMC4414407

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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.