Evidence map›Paper›PMID 34136094›Full record

ArticleComputational and structural biotechnology journal2021

Amino acid residue at the 165th position tunes EYFP chromophore maturation. A structure-based design.

Nadya V Pletneva, Eugene G Maksimov, Elena A Protasova, Anastasia V Mamontova, Tatiana R Simonyan, Rustam H Ziganshin, Konstantin A Lukyanov, Liya Muslinkina, Sergei Pletnev, Alexey M Bogdanov and 1 more

Open access · goldAbstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 24% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Decoding mEos4b day-long maturation and engineering fast-maturing variants.Protein science : a publication of the Protein Society · 2025
    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

11 authors at 4 institutions in 2 countries.

Nadya V PletnevaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Eugene G MaksimovFaculty of Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Elena A ProtasovaFaculty of Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
Anastasia V MamontovaCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow 121205, Russia.
Tatiana R SimonyanCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow 121205, Russia.
Rustam H ZiganshinShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Konstantin A LukyanovCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow 121205, Russia.
Liya MuslinkinaStructural Biology Section, Research Technologies Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Sergei PletnevVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Alexey M BogdanovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Vladimir Z PletnevShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russia.
Institute of Bioorganic Chemistry · RUSkolkovo Institute of Science and Technology · RULomonosov Moscow State University · RUNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the whole GFP family, a few cases, when a single mutation in the chromophore environment strongly inhibits maturation, were described. Here we study EYFP-F165G - a variant of the enhanced yellow fluorescent protein - obtained by a single F165G replacement, and demonstrated multiple fluorescent states represented by the minor emission peaks in blue and yellow ranges (~470 and ~530 nm), and the major peak at ~330 nm. The latter has been assigned to tryptophan fluorescence, quenched due to excitation energy transfer to the mature chromophore in the parental EYFP protein. EYFP-F165G crystal structure revealed two general independent routes of post-translational chemistry, resulting in two main states of the polypeptide chain with the intact chromophore forming triad (~85%) and mature chromophore (~15%). Our experiments thus highlighted important stereochemical role of the 165th position strongly affecting spectral characteristics of the protein. On the basis of the determined EYFP-F165G three-dimensional structure, new variants with ~ 2-fold improved brightness were engineered.

Indexed as

Ala (A), alanineArg (R), arginineAsn (R), asparagineavGFP, Aequorea victoria green fluorescent proteinChromophore maturationDTT, dithiothreitolEC, extinction coefficientEET, excitation energy transferEGFP, enhanced green fluorescent proteinESET, excited-state electron transferExcitation energy transferEYFPEYFP, enhanced yellow fluorescent proteinFemtosecond spectroscopyFLIM, fluorescence lifetime imaging microscopyFluorescent proteinsFP, fluorescent proteinFQY, fluorescence quantum yieldFRET, Förster resonance energy transferFTIR, Fourier-transform infrared (spectroscopyGFP, green fluorescent proteinGln (Q), glutamineGlu (E), glutamic acidGly (G), glycineGYG, glycine-tyrosine-glycineHis (H), histidineIVA-cloning, in vivo assembly cloningLeu (L), leucinePBS, phosphate buffered salinePCR, polymerase chain reactionPhe (F), phenylalanineREACh, resonance energy-accepting chromoproteinSer (S), serinesfGFP, superfolder GFPStructure-guided mutagenesisTrp (W), tryptophanTryptophan fluorescenceTyr (Y), tyrosineVal (V), valineX-ray structure

Identifiers

PMID34136094
PMCPMC8163865
OpenAlexW3161095072

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.