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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Markova S.V., Vysotski E.S., Liu Z.J., Lee J..., Rose J..., Wang B.C.
Заглавие : Crystal structure of a Ca2+-discharged photoprotein - Implications for mechanisms of the calcium trigger and bioluminescence
Колич.характеристики :6 с
Место публикации : J. Biol. Chem.: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2004. - Vol. 279, Is. 32. - С. 33647-33652. - ISSN 0021-9258, DOI 10.1074/jbc.M402427200
Примечания : Cited References: 31
Предметные рубрики: VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
ELECTRON-DENSITY
W92F OBELIN
AEQUORIN
PROTEINS
LIGHT
SEQUENCE
BINDING
COELENTERAZINE
Аннотация: Ca2+-regulated photoproteins are members of the EF-hand calcium-binding protein family. The addition of Ca2+ produces a blue bioluminescence by triggering a decarboxylation reaction of protein-bound hydroperoxycoelenterazine to form the product, coelenteramide, in an excited state. Based on the spatial structures of aequorin and several obelins, we have postulated mechanisms for the Ca2+ trigger and for generation of the different excited states that are the origin of the different colors of bioluminescence. Here we report the crystal structure of the Ca2+-discharged photoprotein obelin at 1.96-Angstrom resolution. The results lend support to the proposed mechanisms and provide new structural insight into details of these processes. Global conformational changes caused by Ca2+ association are typical of the class of calcium signal modulators within the EF-hand protein superfamily. Accommodation of the Ca2+ ions into the loops of the EF-hands is seen to propagate into the active site of the protein now occupied by the coelenteramide where there is a significant repositioning and flipping of the His-175 imidazole ring as crucially required in the trigger hypothesis. Also the H-bonding between His-22 and the coelenterazine found in the active photoprotein is preserved at the equivalent position of coelenteramide, confirming the proposed rapid excited state proton transfer that would lead to the excited state of the phenolate ion pair, which is responsible for the blue emission of bioluminescence.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Titushin M.S., Feng Y.G., Stepanyuk G.A., Li Y..., Markova S.V., Golz S..., Wang B.C., Lee J..., Wang J.F., Vysotski E.S., Liu Z.J.
Заглавие : NMR-derived Topology of a GFP-photoprotein Energy Transfer Complex
Колич.характеристики :10 с
Коллективы :
Место публикации : J. Biol. Chem.: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2010. - Vol. 285, Is. 52. - С. 40891-40900. - ISSN 0021-9258, DOI 10.1074/jbc.M110.133843
Примечания : Cited References: 54. - This work was supported by the National Natural Science Foundation of China, Ministry of Science and Technology of China, CAS Research Grant, CAS Fellowship for Young International Scientists Grant, Russian Foundation for Basic Research (08-09-92209 RFBR-China joint grant), SB RAS Grant 2, "Molecular and Cell Biology" program of RAS, Bayer AG (Germany), and by the University of Georgia Research Foundation and the Georgia Research Alliance.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
STRUCTURAL DETERMINANTS
RENILLA BIOLUMINESCENCE
ANGSTROM RESOLUTION
CRYSTAL-STRUCTURE
ELECTRON-DENSITY
SOFTWARE
PROGRAM
BINDING
SYSTEM
Аннотация: Forster resonance energy transfer within a protein-protein complex has previously been invoked to explain emission spectral modulation observed in several bioluminescence systems. Here we present a spatial structure of a complex of the Ca2+ regulated photoprotein clytin with its green-fluorescent protein (cgGFP) from the jellyfish Clytia gregaria, and show that it accounts for the bioluminescence properties of this system in vitro. We adopted an indirect approach of combining x-ray crystallography determined structures of the separate proteins, NMR spectroscopy, computational docking, and mutagenesis. Heteronuclear NMR spectroscopy using variously N-15, C-13, H-2-enriched proteins enabled assignment of backbone resonances of more than 94% of the residues of both proteins. In a mixture of the two proteins at millimolar concentrations, complexation was inferred from perturbations of certain H-1-N-15 HSQC-resonances, which could be mapped to those residues involved at the interaction site. A docking computation using HADDOCK was employed constrained by the sites of interaction, to deduce an overall spatial structure of the complex. Contacts within the clytin-cgGFP complex and electrostatic complementarity of interaction surfaces argued for a weak protein-protein complex. A weak affinity was also observed by isothermal titration calorimetry (K-D = 0.9 mM). Mutation of clytin residues located at the interaction site reduced the degree of protein-protein association concomitant with a loss of effectiveness of cgGFP in color-shifting the bioluminescence. It is suggested that this clytin-cgGFP structure corresponds to the transient complex previously postulated to account for the energy transfer effect of GFP in the bioluminescence of aequorin or Renilla luciferase.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Okhonin V..., Krylova S.M., Krylov S.N.
Заглавие : Nonequilibrium capillary electrophoresis of equilibrium mixtures, mathematical model
Колич.характеристики :6 с
Место публикации : Anal. Chem.: AMER CHEMICAL SOC, 2004. - Vol. 76, Is. 5. - P1507-1512. - ISSN 0003-2700, DOI 10.1021/ac035259p
Примечания : Cited References: 24
Предметные рубрики: SURFACE-PLASMON RESONANCE
PROTEIN-DNA INTERACTIONS
FLUORESCENCE POLARIZATION
COMPLEX-FORMATION
BINDING
RECOGNITION
DERIVATIVES
TOOL
Аннотация: We recently introduced a new electrophoretic method, nonequilibrium, capillary electrophoresis of equilibrium mixtures (NECEEM). NECEEM provides a unique way of finding kinetic and equilibrium parameters of the formation of intermolecular complexes from a single electropherogram and allows for the use of weak affinity probes in protein quantitation. In this work, we study theoretical bases of NECEEM by developing a mathematical model for the new method. By solving a system of partial differential equations with diffusion in linear approximation, we found the analytical solution for concentrations of components involved in complex formation as functions of time from the beginning of separation and position in the capillary. The nonnumerical nature of the solution makes it a powerful tool in studying the theoretical foundations of the NECEEM method and modeling experimental results. We demonstrate the use of the model for finding binding parameters of complex formation by nonlinear regression of NECEEM electropherograms obtained experimentally.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., TROFIMOV K.P., VYSOTSKII E.S.
Заглавие : PHYSICOCHEMICAL PROPERTIES OF A PHOTOPROTEIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 10. - С. 1020-1027. - 8. - ISSN 0006-2979
Примечания : Cited References: 36
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
CA-2+
INDICATORS
PROTEIN
BINDING
PURIFICATION
EXTRACTION
Ключевые слова (''Своб.индексиров.''): bioluminescence--ca2+-activated photoprotein--obelin--chromatography--calcium
Аннотация: The photoprotein obelin was isolated and purified to homogeneity (as indicated by sodium dodecyl sulfate polyacrylamide gel electrophoresis) from hydroids of Obelia longissima by gel filtration on Sephadex G-75 fine, ion exchange chromatography on Polysil CA-300 (10 mum), hydrophobic chromatography on Phenyl-Sepharose CL-4B, gel filtration on Sephacryl S-200 superfine, ion exchange chromatography on a Mono Q column at pH 7.0, chromatofocusing on a Mono P column (pH gradient 6.0-4.0), and ion exchange chromatography on a Mono Q column at pH 5.5, 8.8, and 7.0. The molecular weight of the native protein was 30 kD, and that measured in the presence of SDS was 19.8 kD. The specific activity of obelin is 4.9.10(15) quanta/mg protein, pseudo-first-order constant of bioluminescence decay 4 sec-1, and quantum yield 0.16 The range of measurable Ca2+ concentrations is 10(-7) to 10(-5) M. The luminescence spectrum of obelin peaks at 469 nm, and the fluorescence emission maximum of the discharged protein is at 455 nm. The optimum pH for luminescence is between 9.0 and 10.5. The molecular ionization constants are pK1 6.8 and pK2 12.2, and the ionization constants for the active site are pK1 9.1 and pK2 10.2
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., VYSOTSKII E.S., ROZHMANOVA O.M., VORONINA S.G.
Заглавие : THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN AS AN INDICATOR OF CALCIUM-TRANSPORT IN PROTEOLIPOSOMES CONTAINING MEMBRANES OF THE T-SYSTEM OF SKELETAL-MUSCLES
Колич.характеристики :5 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1991. - Vol. 56, Is. 5. - С. 546-550. - ISSN 0006-2979
Примечания : Cited References: 12
Предметные рубрики: CHANNEL
CA-2+
MODULATION
BINDING
Ключевые слова (''Своб.индексиров.''): ca2+-transport--ca2+-activated photoprotein obelin--t-system--1,4-dihydropyridines--liposomes
Аннотация: Data are presented on the Ca2+-activated photoprotein obelin as an indicator of calcium transport in proteoliposomes. Proteoliposomes formed from lecithin and membranes of the T-system of rabbit skeletal muscles were found to exhibit permeability to calcium ions activated by 10(-5) M BAU K-8644; 5.10(-5) M nitrendipine inhibits the action of BAU K-8644. Liposomes did not exhibit sensitivity to the investigated agents. The Ca2+-activated photoprotein obelin is a promising tool for studying fast calcium currents.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova, Ludmila P., Lyakhovich, Maria S., Mineev, Konstantin S., Petushkov, Valentin N., Zagitova, Renata, I, Tsarkova, Aleksandra S., Kovalchuk, Sergey, I, Yampolsky, Ilia, V, Vysotski, Eugene S., Kaskova, Zinaida M.
Заглавие : Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation
Колич.характеристики :4 с
Коллективы : Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085]; Russian Foundation for Basic Research, Krasnoyarsk Territory [20-44-242003]; Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds; Russian Science FoundationRussian Science Foundation (RSF) [17-1401169p]; Russian FederationRussian Federation [LS-2605.2020.4]
Место публикации : Org. Lett.: AMER CHEMICAL SOC, 2021. - Vol. 23, Is. 17. - С. 6846-6849. - ISSN 1523-7060, DOI 10.1021/acs.orglett.1c02410. - ISSN 1523-7052(eISSN)
Примечания : Cited References:20. - This work was supported by grant 20-04-00085 of the Russian Foundation for Basic Research, grant 20-44-242003 of the Russian Foundation for Basic Research, Krasnoyarsk Territory, and Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds, grant 17-1401169p of the Russian Science Foundation, and the President of Russian Federation grant for Leading Scientific Schools LS-2605.2020.4 in part of structural elucidation of native products and organic synthesis. We thank Konstantin Antonov (IBCh RAS) and Igor Ivanov (IBCh RAS) for the registration of HRMS spectra.
Предметные рубрики: CRYSTAL-STRUCTURE
BIOLUMINESCENCE
OBELIN
RESIDUES
BINDING
Аннотация: Ca2+-regulated photoproteins of ctenophores lose bioluminescence activity when exposed to visible light. Little is known about the chemical nature of chromophore photo-inactivation. Using a total synthesis strategy, we have established the structures of two unusual coelenterazine products, isolated from recombinant berovin of the ctenophore Beroe abyssicola, which are Z/E isomers. We propose that during light irradiation, these derivatives are formed from 2-hydroperoxycoelenterazine via the intermediate 8a-peroxide by a mechanism reminiscent of that previously described for the auto-oxidation of green-fluorescent-protein-like chromophores.
WOS
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