4ZBL
Phototoxic fluorescent protein mKillerOrange
Summary for 4ZBL
Entry DOI | 10.2210/pdb4zbl/pdb |
Related | 3GB3 3WCK |
Descriptor | KillerOrange, CITRIC ACID, GLYCEROL, ... (4 entities in total) |
Functional Keywords | fluorescent protein, phototoxicity, beta-barrel, qwg chromophore |
Biological source | Hydrozoa (hydrozoans) |
Total number of polymer chains | 1 |
Total formula weight | 27455.75 |
Authors | Pletnev, V.Z.,Pletneva, N.V.,Pletnev, S.V. (deposition date: 2015-04-14, release date: 2015-12-23, Last modification date: 2024-11-06) |
Primary citation | Pletneva, N.V.,Pletnev, V.Z.,Sarkisyan, K.S.,Gorbachev, D.A.,Egorov, E.S.,Mishin, A.S.,Lukyanov, K.A.,Dauter, Z.,Pletnev, S. Crystal Structure of Phototoxic Orange Fluorescent Proteins with a Tryptophan-Based Chromophore. Plos One, 10:e0145740-e0145740, 2015 Cited by PubMed Abstract: 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. PubMed: 26699366DOI: 10.1371/journal.pone.0145740 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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