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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Natashin P.V., Markova S.V., Lee J., Vysotski E.S., Liu Z.-J.
Заглавие : Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins
Место публикации : FEBS J. - 2014. - Vol. 281, Is. 5. - С. 1432-1445. - ISSN 17424658 (ISSN) , DOI 10.1111/febs.12715
Ключевые слова (''Своб.индексиров.''): aequorin--bioluminescence--coelenterazine, obelin--6 (4 hydroxyphenyl) derivative--aequorin--benzene derivative--calcium ion--hydromedusan--mutant protein--obelin--oxygen--photoprotein--unclassified drug--amino acid substitution--article--bioluminescence--calcium transport--crystal structure--fluorescence--hydrogen bond--priority journal--protein conformation--protein structure--wild type--coelenterata--aequorin--bioluminescence--ca2+-regulated photoprotein--coelenterazine, obelin--amino acid substitution--animals--conserved sequence--crystallography, x-ray--hydrogen bonding--hydrozoa--luminescent proteins--models, molecular--mutagenesis, site-directed--mutant proteins--protein conformation--spectrophotometry
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2- hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins. Comparison of spatial structures and the hydrogen bond network formed into the substrate-binding cavity of WT obelin, F88Y obelin, and aequorin clearly shows that the main cause determining different light emission colors of hydromedusan photoproteins is a different arrangement of the hydrogen-bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine due to the presence of either Phe or Tyr residue. © 2014 FEBS.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tomilin F.N., Antipina L.Yu., Vysotski E.S., Ovchinnikov S.G., Gitelzon I.I.
Заглавие : Fluorescence of calcium-discharged obelin: The structure and molecular mechanism of emitter formation
Место публикации : Doklady Biochemistry and Biophysics. - 2008. - Vol. 422, Is. 1. - С. 279-284. - ISSN 16076729 (ISSN) , DOI 10.1134/S1607672908050086
Ключевые слова (''Своб.индексиров.''): calcium--obelin--photoprotein--article--chemical model--chemical structure--chemistry--computer simulation--light--protein binding--protein conformation--radiation exposure--calcium--computer simulation--light--luminescent proteins--models, chemical--models, molecular--protein binding--protein conformation
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