All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin.
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.
Deng
Lu
L
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Vysotski
Eugene S
ES
Markova
Svetlana V
SV
Liu
Zhi-Jie
ZJ
Lee
John
J
Rose
John
J
Wang
Bi-Cheng
BC
D000331:Aequorin / Q000737:chemistry / Q000378:metabolism*; D020816:Amino Acid Motifs; D002118:Calcium / Q000378:metabolism*; D008164:Luminescent Proteins / Q000737:chemistry / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D008164:Luminescent Proteins; C010497:obelin; D000331:Aequorin; D002118:Calcium