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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Burakova, Ludmila P. Natashin, Pavel V. Malikova, Natalia P. Niu, Fengfeng Pu, Mengchen Vysotski, Eugene S. Liu, Zhi-Jie |
| Description | Author Affiliation: Burakova LP ( Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming 650500, China); Natashin PV ( Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming 650500, China); Malikova NP ( Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Bldg. 50, Krasnoyarsk 660036, Russia.); Niu F ( National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China); Pu M ( National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.); Vysotski ES ( Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Bldg. 50, Krasnoyarsk 660036, Russia. Electronic address: eugene.vysotski@gmail.com.); Liu ZJ ( Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming 650500, China) |
| Abstract | Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca(2+)-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca(2+)-binding sites and consequently belongs to a large family of the EF-hand Ca(2+)-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg(2+) determined at 1.75Å. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg(2+) distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca(2+)-binding loops participates in the magnesium ion coordination, it was suggested that Ca(2+)-binding loops of berovin belong to the mixed Ca(2+)/Mg(2+) rather than Ca(2+)-specific type. In addition, we report an effect of physiological concentration of Mg(2+) on bioluminescence of berovin (sensitivity to Ca(2+), rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg(2+) on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca(2+)-binding sites of these photoproteins to Mg(2+). |
| File Format | HTM / HTML |
| ISSN | 10111344 |
| Volume Number | 154 |
| e-ISSN | 18732682 |
| Journal | Journal of Photochemistry and Photobiology B: Biology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-01-01 |
| Publisher Place | Switzerland |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biology Calcium Chemistry Light Luminescent Proteins Metabolism Magnesium Aequorin Amino Acid Sequence Animals Binding Sites Crystallography, X-ray Ctenophora Ions Kinetics Luminescent Measurements Molecular Dynamics Simulation Protein Precursors Protein Structure, Tertiary Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Radiology, Nuclear Medicine and Imaging Biophysics Radiological and Ultrasound Technology Radiation |
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