Тип публикации: статья из журнала
Год издания: 2013
Идентификатор DOI: 10.1016/j.bbapap.2013.07.006
Ключевые слова: Coelenterazine, Calcium, Bioluminescence, Luciferase, Coelenterazine Calcium Bioluminescence Luciferase, 2 hydroperoxycoelenterazine, amino acid, apoprotein, berovin, calcium ion, globular protein, oxygen, photoprotein, unclassified drug, absorption spectroscopy, alkalinity, amino acid sequence, article, Ctenophora, geometry, light, nonhuman, nucleotide sequence, priority journal, protein conformation, Amino Acids, Animals, Apoproteins, Crystallography, X-Ray, Escherichia coli, Hydrogen-Ion Concentration, Imidazoles, Luminescent Measurements, Luminescent Proteins, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Pyrazines, Recombinant Proteins, Sequence Alignment, Beroe abyssicola, Ctenophora (coelenterates)
Аннотация: The bright bioluminescence of ctenophores, found in oceans worldwide, is determined by Ca2+-regulated photoproteins, functionally identical to and sharing many properties of hydromedusan photoproteins. In contrast, however, the ctenophore photoproteins are extremely sensitive to UV and visible light over the range of their absorptiПоказать полностьюon spectrum. The spatial structure of a novel light-sensitive photoprotein from the ctenophore Beroe abyssicola in its apoform bound with three calcium ions is determined at 2.0 angstrom. We demonstrate that the apoberovin is a slightly asymmetrical compact globular protein formed by two domains with a cavity in the center, which exactly retains the fold architecture characteristic of hydromedusan photoproteins despite their low amino acid sequence identity. However, the structural alignment of these two photoprotein classes clearly shows that despite the high similarity of shape and geometry of their coelenterazine-binding cavities, their interiors differ drastically. The key residues appearing to be crucial for stabilizing the 2-hydroperoxycoelenterazine and for formation of the emitter in hydromedusan photoproteins, are replaced in berovin by amino acid residues having completely different side chain properties. Evidently, these replacements must be responsible for the distinct properties of ctenophore photoproteins such as sensitivity to light or the fact that the formation of active photoprotein from apophotoprotein, coelenterazine, and oxygen is more effective at alkaline pH. (C) 2013 Elsevier B.V. All rights reserved.
Журнал: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Выпуск журнала: Vol. 1834, Is. 10
Номера страниц: 2139-2146
ISSN журнала: 15709639
Место издания: AMSTERDAM
Издатель: ELSEVIER SCIENCE BV