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Crystal structure of the fluorescent protein from Dendronephthya sp. in both green and photoconverted red forms.Acta Crystallogr D Struct Biol. 2016 08; 72(Pt 8):922-32.AC
Abstract
The fluorescent protein from Dendronephthya sp. (DendFP) is a member of the Kaede-like group of photoconvertible fluorescent proteins with a His62-Tyr63-Gly64 chromophore-forming sequence. Upon irradiation with UV and blue light, the fluorescence of DendFP irreversibly changes from green (506 nm) to red (578 nm). The photoconversion is accompanied by cleavage of the peptide backbone at the C(α)-N bond of His62 and the formation of a terminal carboxamide group at the preceding Leu61. The resulting double C(α)=C(β) bond in His62 extends the conjugation of the chromophore π system to include imidazole, providing the red fluorescence. Here, the three-dimensional structures of native green and photoconverted red forms of DendFP determined at 1.81 and 2.14 Å resolution, respectively, are reported. This is the first structure of photoconverted red DendFP to be reported to date. The structure-based mutagenesis of DendFP revealed an important role of positions 142 and 193: replacement of the original Ser142 and His193 caused a moderate red shift in the fluorescence and a considerable increase in the photoconversion rate. It was demonstrated that hydrogen bonding of the chromophore to the Gln116 and Ser105 cluster is crucial for variation of the photoconversion rate. The single replacement Gln116Asn disrupts the hydrogen bonding of Gln116 to the chromophore, resulting in a 30-fold decrease in the photoconversion rate, which was partially restored by a further Ser105Asn replacement.
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MeSH
Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Intramural
Research Support, N.I.H., Extramural
Language
eng
PubMed ID
27487823
Citation
Pletneva, Nadya V., et al. "Crystal Structure of the Fluorescent Protein From Dendronephthya Sp. in Both Green and Photoconverted Red Forms." Acta Crystallographica. Section D, Structural Biology, vol. 72, no. Pt 8, 2016, pp. 922-32.
Pletneva NV, Pletnev S, Pakhomov AA, et al. Crystal structure of the fluorescent protein from Dendronephthya sp. in both green and photoconverted red forms. Acta Crystallogr D Struct Biol. 2016;72(Pt 8):922-32.
Pletneva, N. V., Pletnev, S., Pakhomov, A. A., Chertkova, R. V., Martynov, V. I., Muslinkina, L., Dauter, Z., & Pletnev, V. Z. (2016). Crystal structure of the fluorescent protein from Dendronephthya sp. in both green and photoconverted red forms. Acta Crystallographica. Section D, Structural Biology, 72(Pt 8), 922-32. https://doi.org/10.1107/S205979831601038X
Pletneva NV, et al. Crystal Structure of the Fluorescent Protein From Dendronephthya Sp. in Both Green and Photoconverted Red Forms. Acta Crystallogr D Struct Biol. 2016;72(Pt 8):922-32. PubMed PMID: 27487823.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Crystal structure of the fluorescent protein from Dendronephthya sp. in both green and photoconverted red forms.
AU - Pletneva,Nadya V,
AU - Pletnev,Sergei,
AU - Pakhomov,Alexey A,
AU - Chertkova,Rita V,
AU - Martynov,Vladimir I,
AU - Muslinkina,Liya,
AU - Dauter,Zbigniew,
AU - Pletnev,Vladimir Z,
Y1 - 2016/07/13/
PY - 2016/04/07/received
PY - 2016/06/27/accepted
PY - 2016/8/5/entrez
PY - 2016/8/5/pubmed
PY - 2017/10/25/medline
KW - DendFP
KW - DendGFP
KW - DendRFP
KW - Dendronephthya
KW - chromophore
KW - fluorescent photoconvertible proteins
KW - green fluorescent protein
KW - red fluorescent protein
KW - structure–function relationships
KW - three-dimensional structure
KW - β-barrel
SP - 922
EP - 32
JF - Acta crystallographica. Section D, Structural biology
JO - Acta Crystallogr D Struct Biol
VL - 72
IS - Pt 8
N2 - The fluorescent protein from Dendronephthya sp. (DendFP) is a member of the Kaede-like group of photoconvertible fluorescent proteins with a His62-Tyr63-Gly64 chromophore-forming sequence. Upon irradiation with UV and blue light, the fluorescence of DendFP irreversibly changes from green (506 nm) to red (578 nm). The photoconversion is accompanied by cleavage of the peptide backbone at the C(α)-N bond of His62 and the formation of a terminal carboxamide group at the preceding Leu61. The resulting double C(α)=C(β) bond in His62 extends the conjugation of the chromophore π system to include imidazole, providing the red fluorescence. Here, the three-dimensional structures of native green and photoconverted red forms of DendFP determined at 1.81 and 2.14 Å resolution, respectively, are reported. This is the first structure of photoconverted red DendFP to be reported to date. The structure-based mutagenesis of DendFP revealed an important role of positions 142 and 193: replacement of the original Ser142 and His193 caused a moderate red shift in the fluorescence and a considerable increase in the photoconversion rate. It was demonstrated that hydrogen bonding of the chromophore to the Gln116 and Ser105 cluster is crucial for variation of the photoconversion rate. The single replacement Gln116Asn disrupts the hydrogen bonding of Gln116 to the chromophore, resulting in a 30-fold decrease in the photoconversion rate, which was partially restored by a further Ser105Asn replacement.
SN - 2059-7983
UR - https://www.unboundmedicine.com/medline/citation/27487823/Crystal_structure_of_the_fluorescent_protein_from_Dendronephthya_sp__in_both_green_and_photoconverted_red_forms_
L2 - http://scripts.iucr.org/cgi-bin/paper?S205979831601038X
DB - PRIME
DP - Unbound Medicine
ER -
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