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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Burakova L.P., Golz S..., Malikova N.P., Frank L.A., Vysotski E.S.
Заглавие : The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein
Колич.характеристики :15 с
Место публикации : FEBS J.: WILEY-BLACKWELL, 2012. - Vol. 279, Is. 5. - С. 856-870. - ISSN 1742-464X, DOI 10.1111/j.1742-4658.2012.08476.x
Примечания : Cited References: 63. - The authors thank Natalia Chervyakova from Department of Zoology of Invertebrates of Moscow State University for the photo of the White Sea ctenophore Beroe abyssicola. This work was supported by RFBR grant 09-04-00172, by grant 64987.2010.4, Molecular and Cellular Biology program of RAS, and Bayer Pharma AG (Germany).
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
C-TERMINAL PROLINE
SEQUENCE-ANALYSIS
MNEMIOPSIS-SP
COELENTERAZINE-BINDING
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
CRYSTAL-STRUCTURES
EXCITED-STATE
CDNA CLONING
Ключевые слова (''Своб.индексиров.''): bioluminescence--calcium--coelenterazine--luciferase--mammalian expression
Аннотация: Light-sensitive Ca2+-regulated photoproteins are responsible for the bright bioluminescence of ctenophores. Using functional screening, four full-size cDNA genes encoding the same 208-amino-acid polypeptide were isolated from two independent cDNA libraries prepared from two Beroe abyssicola specimens. Sequence analysis revealed three canonical EF-hand calcium-binding sites characteristic of Ca2+-regulated photoproteins, but a very low degree of sequence identity (2729%) with aequorin-type photoproteins, despite functional similarities. Recombinant berovin was expressed in Escherichia coli cells, purified, converted to active photoprotein and characterized. Active berovin has absorption maxima at 280 and 437 nm. The Ca2+-discharged protein loses visible absorption, but exhibits a new absorption maximum at 335 nm. The berovin bioluminescence is blue (?max = 491 nm) and a change in pH over the range 6.09.5 has no significant effect on the light emission spectrum. By contrast, the fluorescence of Ca2+-discharged protein (?ex = 350 nm) is pH sensitive: at neutral pH the maximum is at 420 nm and at alkaline pH there are two maxima at 410 and 485 nm. Like native ctenophore photoproteins, recombinant berovin is also inactivated by light. The Ca2+ concentrationeffect curve is a sigmoid with a slope on a loglog plot of similar to 2.5. Although this curve for berovin is very similar to those obtained for obelin and aequorin, there are evident distinctions: berovin responds to calcium changes at lower concentrations than jellyfish photoproteins and its Ca2+-independent luminescence is low. Recombinant berovin was successfully expressed in mammalian cells, thereby demonstrating potential for monitoring intracellular calcium.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Vysotski E.S., Chen C.J., Rose J.P., Lee J..., Wang B.C.
Заглавие : Structure of the Ca2+-regulated photoprotein obelin at 1.7 angstrom resolution determined directly from its sulfur substructure
Колич.характеристики :9 с
Место публикации : Protein Sci.: CAMBRIDGE UNIV PRESS, 2000. - Vol. 9, Is. 11. - С. 2085-2093. - ISSN 0961-8368
Примечания : Cited References: 41
Предметные рубрики: CALCIUM-MODULATED PROTEINS
AMINO-ACID SEQUENCE
CA-2+-BINDING PHOTOPROTEIN
CA2+-BINDING PHOTOPROTEIN
MACROMOLECULAR STRUCTURES
3-DIMENSIONAL STRUCTURE
ANOMALOUS SCATTERING
CRYSTAL-STRUCTURES
DIFFRACTION DATA
BINDING SITE
Ключевые слова (''Своб.индексиров.''): bioluminescence--crystallography--obelin--photoprotein--single wavelength anomalous scattering--solvent flattening--sulfur phasing
Аннотация: The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 Angstrom resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Stepanyuk G.A., Liu Z.J., Vysotski E.S., Lee J..., Rose J.P., Wang B.C.
Заглавие : Structure based mechanism of the Ca2+ -induced release of coelenterazine from the Renilla binding protein
Колич.характеристики :11 с
Место публикации : Proteins: WILEY-BLACKWELL, 2009. - Vol. 74, Is. 3. - С. 583-593. - ISSN 0887-3585, DOI 10.1002/prot.22173
Примечания : Cited References: 26
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
CRYSTAL-STRUCTURES
RENIFORMIS
LUCIFERASE
BIOLUMINESCENCE
PURIFICATION
ANGSTROM
MUELLERI
Ключевые слова (''Своб.индексиров.''): bioluminescence--ef-hand--coelenteramider--luciferase--ca2+-binding protein
Аннотация: The crystal structure of the Ca2+-loaded coelenterazine binding protein from Renilla muelleri in its apo-state has been determined at resolution 1.8 angstrom. Although calcium binding hardly affects the compact scaffold and overall fold of the structure before calcium addition, there are easily discerned shifts in the residues that were interacting with the coelenterazine and a repositioning of helices, to expose a cavity to the external solvent. Altogether these changes offer a straightforward explanation for how following the addition of Ca2+, the coelenterazine could escape and become available for bioluminescence on Renilla luciferase. A docking computation supports the possibility of a luciferase-binding protein complex.
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