ArticleProceedings of the National Academy of Sciences of the United States of America2005
Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 57 citations in OpenAlex.
- Bioluminescence of the heterotrophic dinoflagellate Polykrikos kofoidii Chatton 1914 (Dinophyceae).Journal of phycology · 2026Article
- Bioluminescence in Clinical and Point-of-Care Testing.Biosensors · 2025Review
- Bioluminescent Dinoflagellates as a Bioassay for Toxicity Assessment.International journal of molecular sciences · 2022Review
- Bioluminescence and Photoreception in Unicellular Organisms: Light-Signalling in a Bio-Communication Perspective.International journal of molecular sciences · 2021Review
- Lipocalin Blc is a potential heme-binding protein.FEBS letters · 2021Article
- New Perspectives Related to the Bioluminescent System in Dinoflagellates:International journal of molecular sciences · 2020Review
- Mechanosensitivity of a rapid bioluminescence reporter system assessed by atomic force microscopy.Biophysical journal · 2015Article
- Structure and mechanism of the phycobiliprotein lyase CpcT.The Journal of biological chemistry · 2014Article
- Understanding Bioluminescence in Dinoflagellates-How Far Have We Come?Microorganisms · 2013Review
- Protein-protein complexation in bioluminescence.Protein & cell · 2011Review
- On the origin of fluorescence in bacteriophytochrome infrared fluorescent proteins.The journal of physical chemistry. B · 2010Article
- Profile of J. Woodland Hastings.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The luciferase of Lingulodinium polyedrum, a marine bioluminescent dinoflagellate, consists of three similar but not identical domains in a single polypeptide. Each encodes an active luciferase that catalyzes the oxidation of a chlorophyll-derived open tetrapyrrole (dinoflagellate luciferin) to produce blue light. These domains share no sequence similarity with any other in the GenBank database and no structural or motif similarity with any other luciferase. We report here the 1.8-A crystal structure of the third domain, D3, at pH 8, and a mechanism for its activity regulation by pH. D3 consists of two major structural elements: a beta-barrel pocket putatively for substrate binding and catalysis and a regulatory three-helix bundle. N-terminal histidine residues previously shown to regulate activity by pH are at the interface of the helices in the bundle. Molecular dynamics calculations indicate that, in response to changes in pH, these histidines could trigger a large molecular motion of the bundle, thereby exposing the active site to the substrate.
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