Preparation and X-ray crystallographic analysis of the Ca2+-discharged photoprotein obelin

Authors: Deng, Lu; Markova, Svetlana V.; Vysotski, Eugene S.; Liu, Zhi-Jie; Lee, John; Rose, John; Wang, Bi-Cheng

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 512-514(3)

Publisher: Blackwell Publishing

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Abstract:

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 P43212 or P41212. The unit-cell parameters are a = b = 53.4, c = 144.0 Å. The crystals diffract to 1.9 Å resolution.

Document Type: Research article

DOI: 10.1107/S090744490302852X

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