ArticleProtein science : a publication of the Protein Society2005
All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 93 citations in OpenAlex.
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- 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
- In vitro CBArchives of toxicology · 2025Article
- Bioluminescence in Clinical and Point-of-Care Testing.Biosensors · 2025Review
- Design of Ctenophore CaLife (Basel, Switzerland) · 2024Article
- Off-target activity of NBOMes and NBOMe analogs at the µ opioid receptor.Archives of toxicology · 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 semisynthetic obelin-v.Protein science : a publication of the Protein Society · 2022Article
- The X-ray structure of juvenile hormone diol kinase from the silkworm Bombyx mori.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Cardioluminescence in Transgenic Zebrafish Larvae: A Calcium Imaging Tool to Study Drug Effects and Pathological Modeling.Biomedicines · 2021Article
- 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
- RedquorinXS Mutants with Enhanced Calcium Sensitivity and Bioluminescence Output Efficiently Report Cellular and Neuronal Network Activities.International journal of molecular sciences · 2020Article
- Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents.International journal of molecular sciences · 2020Article
- Article
- 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
- Genomic organization, evolution, and expression of photoprotein and opsin genes in Mnemiopsis leidyi: a new view of ctenophore photocytes.BMC biology · 2012Article
- Protein-protein complexation in bioluminescence.Protein & cell · 2011Review
- Prediction of calcium-binding sites by combining loop-modeling with machine learning.BMC structural biology · 2009Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7A and 2.2 A, respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hyroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with product, coleneteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.
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