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PDBsum entry 6nqs
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Fluorescent protein
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PDB id
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6nqs
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PDB id:
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| Name: |
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Fluorescent protein
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Title:
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Crystal structure of fast switching m159t mutant of fluorescent protein dronpa (dronpa2)- y63(3-omey)
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Structure:
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Fluorescent protein dronpa. Chain: a, b, c, d, e, f, g, h. Engineered: yes. Mutation: yes
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Source:
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Echinophyllia sp. Sc22. Organism_taxid: 301887. Gene: dronpa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
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Resolution:
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2.50Å
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R-factor:
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0.215
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R-free:
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0.251
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Authors:
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C.-Y.Lin,M.G.Romei,I.I.Mathews,S.G.Boxer
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Key ref:
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M.G.Romei
et al.
(2020).
Electrostatic control of photoisomerization pathways in proteins.
Science,
367,
76-79.
PubMed id:
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Date:
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21-Jan-19
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Release date:
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12-Jun-19
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PROCHECK
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Headers
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References
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Q5TLG6
(Q5TLG6_9CNID) -
Fluorescent protein Dronpa from Echinophyllia sp. SC22
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Seq:
Struc:
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224 a.a.
222 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 5 residue positions (black
crosses)
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Science
367:76-79
(2020)
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PubMed id:
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Electrostatic control of photoisomerization pathways in proteins.
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M.G.Romei,
C.Y.Lin,
I.I.Mathews,
S.G.Boxer.
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ABSTRACT
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Rotation around a specific bond after photoexcitation is central to vision and
emerging opportunities in optogenetics, super-resolution microscopy, and
photoactive molecular devices. Competing roles for steric and electrostatic
effects that govern bond-specific photoisomerization have been widely discussed,
the latter originating from chromophore charge transfer upon excitation. We
systematically altered the electrostatic properties of the green fluorescent
protein chromophore in a photoswitchable variant, Dronpa2, using amber
suppression to introduce electron-donating and electron-withdrawing groups to
the phenolate ring. Through analysis of the absorption (color), fluorescence
quantum yield, and energy barriers to ground- and excited-state isomerization,
we evaluate the contributions of sterics and electrostatics quantitatively and
demonstrate how electrostatic effects bias the pathway of chromophore
photoisomerization, leading to a generalized framework to guide protein design.
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Links
