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Ca2+-regulated photoproteins: Structural insight into the bioluminescence mechanism [Text] / E. S. Vysotski, J. . Lee // Accounts Chem. Res. - 2004. - Vol. 37, Is. 6. - P405-415, DOI 10.1021/ar0400037. - Cited References: 44 . - ISSN 0001-4842

РУБ Chemistry, Multidisciplinary
Рубрики:
AEQUORIN BIOLUMINESCENCE
   SEQUENCE-ANALYSIS
   CALCIUM-BINDING
   CA2+-BINDING PHOTOPROTEIN
   VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   FUNCTIONAL PART
   EXCITED-STATES
   W92F OBELIN
   COELENTERAZINE
Аннотация: The bioluminescent jellyfish has contributed two famous proteins to modern science: green fluorescent protein or GFP, which finds wide use as a probe in cell biology studies, and aequorin, which has been used for intracellular calcium measurement for more than 30 years. More recently, obelin, a protein from the bioluminescent hydroid and also in the family of what are called "Ca2+-regulated photoproteins", has been shown to have very attractive properties both in general applications and for basic structural biology investigations. This review will survey the new information into their molecular mechanism of bioluminescence action.

Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Lee, J...

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Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and after bioluminescence support the catalytic function of a water molecule in the reaction [Text] / P. V. Natashin [et al.] // Acta Crystallogr. Sect. D-Biol. Crystallogr. - 2014. - Vol. 70. - P720-732, DOI 10.1107/S1399004713032434. - Cited References: 71. - We acknowledge the use of beamline BL17U1 at the Shanghai Synchrotron Radiation Facility, China. This work was supported by RFBR grants 12-04-91153, 12-04-00131 and the China-Russia International Collaboration grant from the Chinese Academy of Sciences and NSFC, by the Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' (grant 11.G34.31.0058) and 'Molecular and Cellular Biology' of the RAS, the President of the Russian Federation 'Leading Science School' (grant 3951.2012.4). PVN and EVE were supported by RFBR grant 14-04-31092. . - ISSN 0907-4449. - ISSN 1399-0047

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Biophysics + Crystallography
Рубрики:
AEQUORIN BIOLUMINESCENCE
   SEQUENCE-ANALYSIS
   CRYSTAL-STRUCTURE
   CA2+-BINDING PHOTOPROTEIN
   VIOLET BIOLUMINESCENCE
   CALCIUM CONCENTRATION
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   MNEMIOPSIS-LEIDYI
   EXCITED-STATES
Аннотация: Ca2+-regulated photoproteins, which are responsible for light emission in a variety of marine coelenterates, are a highly valuable tool for measuring Ca2+ inside living cells. All of the photoproteins are a single-chain polypeptide to which a 2-hydroperoxycoelenterazine molecule is tightly but noncovalently bound. Bioluminescence results from the oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. Here, the crystal structures of the Y138F obelin mutant before and after bioluminescence are reported at 1.72 and 1.30 angstrom resolution, respectively. The comparison of the spatial structures of the conformational states of Y138F obelin with those of wild-type obelin gives clear evidence that the substitution of Tyr by Phe does not affect the overall structure of both Y138F obelin and its product following Ca2+ discharge compared with the corresponding conformational states of wild-type obelin. Despite the similarity of the overall structures and internal cavities of Y138F and wild-type obelins, there is a substantial difference: in the cavity of Y138F obelin a water molecule corresponding to W2 in wild-type obelin is not found. However, in Ca2+-discharged Y138F obelin this water molecule now appears in the same location. This finding, together with the observed much slower kinetics of Y138F obelin, clearly supports the hypothesis that the function of a water molecule in this location is to catalyze the 2-hydroperoxycoelenterazine decarboxylation reaction by protonation of a dioxetanone anion before its decomposition into the excited-state product. Although obelin differs from other hydromedusan Ca2+-regulated photoproteins in some of its properties, they are believed to share a common mechanism.

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Держатели документа:
[Natashin, Pavel V.
Ding, Wei
Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China
[Natashin, Pavel V.
Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia
[Natashin, Pavel V.
Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Chair Biophys, Krasnoyarsk, Russia
[Ding, Wei] Chinese Acad Sci, Inst Biophys, Ctr Biol Imaging, Beijing 100080, Peoples R China
[Lee, John] Univ Georgia, Dept Biochem Mol Biol, Athens, GA 30602 USA
[Liu, Zhi-Jie] Shanghai Tech Univ, Human Inst, Shanghai, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Natashin, P.V.; Ding, W...; Eremeeva, E.V.; Markova, S.V.; Lee, J...; Vysotski, E.S.; Liu, Z.J.; RFBR [12-04-91153, 12-04-00131, 14-04-31092]; Chinese Academy of Sciences; NSFC; Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' [11.G34.31.0058]; RAS; Russian Federation 'Leading Science School' [3951.2012.4]

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