Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore.
Phototoxic fluorescent proteins represent a sparse group of genetically encoded photosensitizers that could be used for precise light-induced inactivation of target proteins, DNA damage, and cell killing. Only two such GFP-based fluorescent proteins (FPs), KillerRed and its monomeric variant SuperNo...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0145740 |
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| author | Nadya V Pletneva Vladimir Z Pletnev Karen S Sarkisyan Dmitry A Gorbachev Evgeny S Egorov Alexander S Mishin Konstantin A Lukyanov Zbigniew Dauter Sergei Pletnev |
| author_facet | Nadya V Pletneva Vladimir Z Pletnev Karen S Sarkisyan Dmitry A Gorbachev Evgeny S Egorov Alexander S Mishin Konstantin A Lukyanov Zbigniew Dauter Sergei Pletnev |
| author_sort | Nadya V Pletneva |
| collection | DOAJ |
| description | Phototoxic fluorescent proteins represent a sparse group of genetically encoded photosensitizers that could be used for precise light-induced inactivation of target proteins, DNA damage, and cell killing. Only two such GFP-based fluorescent proteins (FPs), KillerRed and its monomeric variant SuperNova, were described up to date. Here, we present a crystallographic study of their two orange successors, dimeric KillerOrange and monomeric mKillerOrange, at 1.81 and 1.57 Å resolution, respectively. They are the first orange-emitting protein photosensitizers with a tryptophan-based chromophore (Gln65-Trp66-Gly67). Same as their red progenitors, both orange photosensitizers have a water-filled channel connecting the chromophore to the β-barrel exterior and enabling transport of ROS. In both proteins, Trp66 of the chromophore adopts an unusual trans-cis conformation stabilized by H-bond with the nearby Gln159. This trans-cis conformation along with the water channel was shown to be a key structural feature providing bright orange emission and phototoxicity of both examined orange photosensitizers. |
| format | Article |
| id | doaj-art-e36b7701a2794df4983a7c5bab7f0b65 |
| institution | OA Journals |
| issn | 1932-6203 |
| language | English |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-e36b7701a2794df4983a7c5bab7f0b652025-08-20T02:22:40ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-011012e014574010.1371/journal.pone.0145740Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore.Nadya V PletnevaVladimir Z PletnevKaren S SarkisyanDmitry A GorbachevEvgeny S EgorovAlexander S MishinKonstantin A LukyanovZbigniew DauterSergei PletnevPhototoxic fluorescent proteins represent a sparse group of genetically encoded photosensitizers that could be used for precise light-induced inactivation of target proteins, DNA damage, and cell killing. Only two such GFP-based fluorescent proteins (FPs), KillerRed and its monomeric variant SuperNova, were described up to date. Here, we present a crystallographic study of their two orange successors, dimeric KillerOrange and monomeric mKillerOrange, at 1.81 and 1.57 Å resolution, respectively. They are the first orange-emitting protein photosensitizers with a tryptophan-based chromophore (Gln65-Trp66-Gly67). Same as their red progenitors, both orange photosensitizers have a water-filled channel connecting the chromophore to the β-barrel exterior and enabling transport of ROS. In both proteins, Trp66 of the chromophore adopts an unusual trans-cis conformation stabilized by H-bond with the nearby Gln159. This trans-cis conformation along with the water channel was shown to be a key structural feature providing bright orange emission and phototoxicity of both examined orange photosensitizers.https://doi.org/10.1371/journal.pone.0145740 |
| spellingShingle | Nadya V Pletneva Vladimir Z Pletnev Karen S Sarkisyan Dmitry A Gorbachev Evgeny S Egorov Alexander S Mishin Konstantin A Lukyanov Zbigniew Dauter Sergei Pletnev Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore. PLoS ONE |
| title | Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore. |
| title_full | Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore. |
| title_fullStr | Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore. |
| title_full_unstemmed | Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore. |
| title_short | Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore. |
| title_sort | crystal structure of phototoxic orange fluorescent proteins with a tryptophan based chromophore |
| url | https://doi.org/10.1371/journal.pone.0145740 |
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