1EL4

STRUCTURE OF THE CALCIUM-REGULATED PHOTOPROTEIN OBELIN DETERMINED BY SULFUR SAS

1EL4 の概要

• エントリーDOI: 10.2210/pdb1el4/pdb
• 分子名称: OBELIN, CHLORIDE ION, C2-HYDROXY-COELENTERAZINE, ... (4 entities in total)
• 機能のキーワード: bioluminescence, calcium, photoprotein, obelin, sulfur anomalous scattering, luminescent protein
• 由来する生物種: Obelia longissima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22729.82

構造登録者

Liu, Z.J.,Vysotski, E.S.,Rose, J.,Lee, J.,Wang, B.C. (登録日: 2000-03-13, 公開日: 2001-03-13, 最終更新日: 2024-02-07)

主引用文献

Liu, Z.J.,Vysotski, E.S.,Chen, C.J.,Rose, J.P.,Lee, J.,Wang, B.C.
Structure of the Ca2+-regulated photoprotein obelin at 1.7 A resolution determined directly from its sulfur substructure.
Protein Sci., 9:2085-2093, 2000

PubMed Abstract: The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 A resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.

PubMed: 11152120

実験手法

X-RAY DIFFRACTION (1.73 Å)