Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins

doi:10.1111/febs.12715

	Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins
	Natashin, Pavel V.1,2,3; Markova, Svetlana V.2,3; Lee, John 4; Vysotski, Eugene S.2,3; Liu, Zhi-Jie1,5
	2014-03
发表期刊	FEBS JOURNAL
ISSN	1742-464X
卷号	281 期号:5 页码:1432-1445
发表状态	已发表
DOI	10.1111/febs.12715
摘要	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 462-495nm, 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 etal. (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.
关键词	aequorin bioluminescence Ca2+-regulated photoprotein coelenterazine obelin
收录类别	SCI
语种	英语
资助项目	Russian Federation 'Leading Science School'[3951.2012.4]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000332083600009
出版者	WILEY
WOS关键词	LIGHT-SENSITIVE PHOTOPROTEIN ; CTENOPHORE BEROE ABYSSICOLA ; SEQUENCE-ANALYSIS ; CA2+-BINDING PHOTOPROTEIN ; VIOLET BIOLUMINESCENCE ; SECONDARY-STRUCTURE ; RECOMBINANT OBELIN ; MNEMIOPSIS-LEIDYI ; W92F OBELIN ; CALCIUM
原始文献类型	Article
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1070
专题	iHuman研究所_PI研究组_刘志杰组 iHuman研究所
通讯作者	Liu, Zhi-Jie
作者单位	1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia 3.Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk, Russia 4.Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA 5.ShanghaiTech Univ, iHuman Inst, Shanghai, Peoples R China
通讯作者单位	iHuman研究所
推荐引用方式 GB/T 7714	Natashin, Pavel V.,Markova, Svetlana V.,Lee, John,et al. Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins[J]. FEBS JOURNAL,2014,281(5):1432-1445.
APA	Natashin, Pavel V.,Markova, Svetlana V.,Lee, John,Vysotski, Eugene S.,&Liu, Zhi-Jie.(2014).Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins.FEBS JOURNAL,281(5),1432-1445.
MLA	Natashin, Pavel V.,et al."Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins".FEBS JOURNAL 281.5(2014):1432-1445.