ArticleProceedings of the National Academy of Sciences of the United States of America2006
Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 89 citations in OpenAlex.
- Fast kinetics of photoprotein emitting species.Scientific reports · 2025Article
- The key residue responsible for the red shift of bioluminescence spectra of light-sensitive CaScientific reports · 2025Article
- Design of Ctenophore CaLife (Basel, Switzerland) · 2024Article
- Illuminating the mechanism and allosteric behavior of NanoLuc luciferase.Nature communications · 2023Article
- The Role of Tyr-His-Trp Triad and Water Molecule Near the N1-Atom of 2-Hydroperoxycoelenterazine in Bioluminescence of Hydromedusan Photoproteins: Structural and Mutagenesis Study.International journal of molecular sciences · 2023Article
- Crystal structure of semi-synthetic obelin-v after calcium induced bioluminescence implies coelenteramine as the main reaction product.Scientific reports · 2022Article
- Crystal structure of semisynthetic obelin-v.Protein science : a publication of the Protein Society · 2022Article
- Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- Rapid and sensitive large-scale screening of low affinity extracellular receptor protein interactions by using reaction induced inhibition of Gaussia luciferase.Scientific reports · 2020Article
- Reaction mechanism of the bioluminescent protein mnemiopsin1 revealed by X-ray crystallography and QM/MM simulations.The Journal of biological chemistry · 2019Article
- QM/MM simulations provide insight into the mechanism of bioluminescence triggering in ctenophore photoproteins.PloS one · 2017Article
- Expression and characterization of the calcium-activated photoprotein from the ctenophore Bathocyroe fosteri: insights into light-sensitive photoproteins.Biochemical and biophysical research communications · 2013Article
- Cloning, sequencing, expression and structural investigation of mnemiopsin from Mnemiopsis leidyi: an attempt toward understanding Ca2+-regulated photoproteins.The protein journal · 2011Article
- Protein-protein complexation in bioluminescence.Protein & cell · 2011Review
- Expression, purification and characterization of the secreted luciferase of the copepod Metridia longa from Sf9 insect cells.Protein expression and purification · 2008Article
- Mutational optimization of the coelenterazine-dependent luciferase from Renilla.Plant methods · 2008Article
- Structure-function studies on the active site of the coelenterazine-dependent luciferase from Renilla.Protein science : a publication of the Protein Society · 2008Article
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7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crystal structure at 1.93-A resolution is determined for the Ca2+-discharged obelin containing three bound calcium ions as well as the product of the bioluminescence reaction, coelenteramide. This finding extends the series of available spatial structures of the ligand-dependent conformations of the protein to four, the obelin itself, and those after the bioluminescence reaction with or without bound Ca2+ and/or coelenteramide. Among these structures, global conformational changes are small, typical of the class of "calcium signal modulators" within the EF-hand protein superfamily. Nevertheless, in the active site there are significant repositions of two residues. The His-175 imidazole ring flips becoming almost perpendicular to the original orientation corroborating the crucial importance of this residue for triggering bioluminescence. Tyr-138 hydrogen bonded to the coelenterazine N1-atom in unreacted obelin is moved away from the binding cavity after reaction. However, this Tyr is displaced by a water molecule from within the cavity, which now forms a hydrogen bond to the same atom, the amide N of coelenteramide. From this observation, a reaction scheme is proposed that would result in the neutral coelenteramide as the primary excited state product in photoprotein bioluminescence. From such a higher energy state it is now energetically feasible to account for the shorter wavelength bioluminescence spectra obtained from some photoprotein mutants or to populate the lower energy state of the phenolate anion to yield the blue bioluminescence ordinarily observed from native photoproteins.
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