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4ZBL

Phototoxic fluorescent protein mKillerOrange

Summary for 4ZBL
Entry DOI10.2210/pdb4zbl/pdb
Related3GB3 3WCK
DescriptorKillerOrange, CITRIC ACID, GLYCEROL, ... (4 entities in total)
Functional Keywordsfluorescent protein, phototoxicity, beta-barrel, qwg chromophore
Biological sourceHydrozoa (hydrozoans)
Total number of polymer chains1
Total formula weight27455.75
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 citationPletneva, 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: 26699366
DOI: 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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