Evidence map›Paper›PMID 25565105›Full record

ArticleStructure (London, England : 1993)2015

A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins.

Hanseong Kim, Taisong Zou, Chintan Modi, Katerina Dörner, Timothy J Grunkemeyer, Liqing Chen, Raimund Fromme, Mikhail V Matz, S Banu Ozkan, Rebekka M Wachter

Open access · greenAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
10.4field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 85 citations in OpenAlex.

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  18. Photoswitchable Fluorescent Proteins: Mechanisms on Ultrafast Timescales.International journal of molecular sciences · 2022
    Review
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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

10 authors at 2 institutions in 1 country.

Hanseong KimDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.
Taisong ZouCenter for Biological Physics, Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
Chintan ModiInstitute for Cellular and Molecular Biology, The University of Texas, Austin, TX 78712, USA.
Katerina DörnerDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.
Timothy J GrunkemeyerDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.
Liqing ChenDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.
Raimund FrommeDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.
Mikhail V MatzSection of Integrative Biology, The University of Texas, Austin, TX 78712, USA.
S Banu OzkanCenter for Biological Physics, Department of Physics, Arizona State University, Tempe, AZ 85287, USA. Electronic address: banu.ozkan@asu.edu.
Rebekka M WachterDepartment of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA; Center for Bioenergy and Photosynthesis, Arizona State University, Tempe, AZ 85287, USA. Electronic address: rwachter@asu.edu.
Arizona State University · USThe University of Texas at Austin · US

Funding

Center for the Rational Design of Membrane Protein CrystallographyU54GM094599 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2014
$6.8M
NIGMS NIH HHS U54 GM094599
6 · The paper itself

Abstract

In proteins, functional divergence involves mutations that modify structure and dynamics. Here we provide experimental evidence for an evolutionary mechanism driven solely by long-range dynamic motions without significant backbone adjustments, catalytic group rearrangements, or changes in subunit assembly. Crystallographic structures were determined for several reconstructed ancestral proteins belonging to a GFP class frequently employed in superresolution microscopy. Their chain flexibility was analyzed using molecular dynamics and perturbation response scanning. The green-to-red photoconvertible phenotype appears to have arisen from a common green ancestor by migration of a knob-like anchoring region away from the active site diagonally across the β barrel fold. The allosterically coupled mutational sites provide active site conformational mobility via epistasis. We propose that light-induced chromophore twisting is enhanced in a reverse-protonated subpopulation, activating internal acid-base chemistry and backbone cleavage to enlarge the chromophore. Dynamics-driven hinge migration may represent a more general platform for the evolution of novel enzyme activities.

Indexed as

Evolution, MolecularProtein FoldingCatalytic DomainColorCrystallography, X-RayFluorescenceGreen Fluorescent ProteinsLuminescent ProteinsModels, MolecularMolecular Dynamics SimulationMotionMutationProtein StabilityProtein Structure, TertiaryRed Fluorescent ProteinGreen Fluorescent ProteinsLuminescent ProteinsRed Fluorescent Protein

Identifiers

PMID25565105
PMCPMC4370283
OpenAlexW2022497131

What OpenQuestion holds

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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.