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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) : Deng L..., Markova S.V., Vysotski E.S., Liu Z.J., Lee J..., Rose J..., Wang B.C.
Заглавие : Preparation and X-ray crystallographic analysis of the Ca2+-discharged photoprotein obelin
Колич.характеристики :3 с
Место публикации : Acta Crystallogr. Sect. D-Biol. Crystallogr.: BLACKWELL MUNKSGAARD, 2004. - Vol. 60. - С. 512-514. - ISSN 0907-4449, DOI 10.1107/S090744490302852X
Примечания : Cited References: 18
Предметные рубрики: VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
W92F OBELIN
AEQUORIN
SEQUENCE
PROTEIN
CLONING
CDNA
Аннотация: Ca2+-regulated photoproteins belong to the EF-hand Ca2+-binding protein family. The addition of calcium ions initiates bright blue bioluminescence of the photoproteins, a result of the oxidative breakdown of coelenterazine peroxide to coelenteramide. Crystals of the Ca2+-discharged W92F mutant of obelin from Obelia longissima have been grown, representing the first crystallization of a photoprotein after the Ca2+-triggered bioluminescence. A green fluorescence observed from the crystals clearly demonstrates that coelenteramide, the bioluminescence product of coelenterazine peroxide, is bound within the protein. The diffraction pattern exhibits tetragonal Laue symmetry. Systematic absences indicate that the space group is either P4(3)2(1)2 or P4(1)2(1)2. The unit-cell parameters are a=b=53.4, c=144.0 Angstrom. The crystals diffract to 1.9 Angstrom resolution.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKII Y.S., BONDAR V.S., GITELZON I.I.
Заглавие : ISOLATION AND PROPERTIES OF VARIOUS MOLECULAR-FORMS OF CA2+-ACTIVATED PHOTOPROTEIN OBELIN
Колич.характеристики :4 с
Место публикации : DOKLADY AKADEMII NAUK SSSR: MEZHDUNARODNAYA KNIGA, 1991. - Vol. 321, Is. 1. - С. 214-217. - ISSN 0002-3264
Примечания : Cited References: 14
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
PROTEIN
PURIFICATION
EXTRACTION
PHIALIDIN
SEQUENCE
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bondar V.S., Purtov K.V., Malikova N.P., Frank L.A., Illarionov B.A.
Заглавие : Role of conservative residue Cys158 in the formation of an active photoprotein complex of obelin
Колич.характеристики :5 с
Место публикации : Biochem.-Moscow: MAIK NAUKA/INTERPERIODICA, 2001. - Vol. 66, Is. 9. - С. 1014-1018. - ISSN 0006-2979, DOI 10.1023/A:1012377827626
Примечания : Cited References: 21
Предметные рубрики: CDNA
EXPRESSION
AEQUORIN
SEQUENCE
CLONING
Ключевые слова (''Своб.индексиров.''): photoproteins--obelin--apoobelin mutants--bioluminescence
Аннотация: Using site directed mutagenesis, the conservative residue Cys158 of recombinant apoobelin was substituted for sera ine (C158S, S-mutant) or alanine (C158A, A-mutant). These point mutations resulted in significant changes in the apoobelin structure accompanied by slowing of photoprotein complex formation, decrease of its stability, and changing of its bioluminescence characteristics. The enzymatic properties of the photoprotein decreased in the series: wild-type protein S-mutant A-mutant. This is consistent with rank of nucleophilicity SH OH CH3 of cysteine, serine, and alanine side chain functional groups, respectively. Possible mechanisms of the involvement of the apoobelin Cys158 SH-group in the formation of the enzyme-substrate complex are considered.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Chiu H.H., Rogozin D.Y., Huang S.P., Degermendzhy A.G., Shieh W.Y., Tang S.L.
Заглавие : Aliidiomarina shirensis sp nov., a halophilic bacterium isolated from Shira Lake in Khakasia, southern Siberia, and a proposal to transfer Idiomarina maris to the genus Aliidiomarina
Колич.характеристики :6 с
Коллективы : National Science Council, Taiwan [NSC 99-2923-B-001-001-MY3]; Russian Foundation for Basic Research [14-04-01060-a]; Siberian Branch of Russian Academy of Sciences, joint Taiwan-Siberian Project [11]
Место публикации : Int. J. Syst. Evol. Microbiol.: SOC GENERAL MICROBIOLOGY, 2014. - Vol. 64. - С. 1334-1339. - ISSN 1466-5026, DOI 10.1099/ijs.0.057851-0. - ISSN 1466-5034
Примечания : Cited References: 22. - We thank Dr Egor S. Zadereev and Dr Vladimir V. Zykov at the Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk, for assistance with sampling. This study was supported by Russia Taiwan joint project funding (NSC 99-2923-B-001-001-MY3) from the National Science Council, Taiwan, the Russian Foundation for Basic Research, Grant No. 14-04-01060-a and Siberian Branch of Russian Academy of Sciences, joint Taiwan-Siberian Project No. 11.
Предметные рубрики: SHALLOW COASTAL WATER
RIBOSOMAL-RNA GENE
EMENDED DESCRIPTION
PSEUDIDIOMARINA
PHYLOTYPES
SEQUENCE
TAIWAN
Аннотация: Strain AIS(T), an aerobic halophilic, Gram-reaction-negative, heterotrophic bacterium isolated from the water of Shira Lake in Khakasia, southern Siberia, was characterized using a polyphasic approach. Our analysis of the 16S rRNA gene sequences showed that 'Aliidiomarina haloalkalitolerans', 'Allidiomarina sanyensis', Idiomarina maris and AIS(T) formed a distinct lineage. The sequence similarities between AIS(T) and the type strains of species of the genera Idiomarina and Aliidiomarina were 91.6-95.1 % and 94.0-96.9 %, respectively. The major isoprenoid quinone of AIS(T) was ubiquinone 8 (Q-8). Predominant cellular fatty acids were iso-C-17:0, iso-C-15:0 and summed feature 9. The genomic DNA G+C content was 45.8 mol%. It is concluded that AIS(T) represents a novel species of the genus Aliidiomarina, and the name Aliidiomarina shirensis sp. nov. is herein proposed for it. The type strain is AIST (=JCM 17761(T)=BCRC 80327(T)). Based on its fatty acid profile and our phylogenetic analysis, we propose that Idiomarina mans be transferred to the genus Aliidiomarina.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Sandalova T.P., Ugarova N.N.
Заглавие : Model of the active site of firefly luciferase
Колич.характеристики :6 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1999. - Vol. 64, Is. 8. - P962-967. - ISSN 0006-2979
Примечания : Cited References: 20
Предметные рубрики: ESCHERICHIA-COLI
SEQUENCE
CLONING
ENZYME
CDNA
SUPERFAMILY
Ключевые слова (''Своб.индексиров.''): bioluminescence--firefly luciferase--atp--luciferin--spatial structure--active site--enzyme-substrate complex
Аннотация: A model for the spatial structure of firefly luciferase-ATP-luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme-substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP-phenylalanine-synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.
WOS
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