NDLI: All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin.

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All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin.

Content Provider	Semantic Scholar
Author	Deng, Lu Vysotski, Eugene S. Markova, Svetlana V. Liu, Zhi-Jie Lee, John Rose, John P. Wang, Bi-Cheng
Copyright Year	2005
Abstract	The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7A and 2.2 A, respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hyroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with product, coleneteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.
File Format	PDF HTM / HTML
DOI	10.1110/ps.041142905
PubMed reference number	15689515
Journal	Medline
Volume Number	14
Issue Number	3
Alternate Webpage(s)	https://kms.shanghaitech.edu.cn/bitstream/2MSLDSTB/1132/1/10.1110@ps.041142905.pdf
Alternate Webpage(s)	https://doi.org/10.1110/ps.041142905
Journal	Protein science : a publication of the Protein Society
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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