1QV0

Atomic resolution structure of obelin from Obelia longissima

1QV0 の概要

• エントリーDOI: 10.2210/pdb1qv0/pdb
• 関連するPDBエントリー: 1EJ3 1EL4 1JF0 1JF2 1QV1
• 分子名称: Obelin, COBALT (II) ION, POTASSIUM ION, ... (6 entities in total)
• 機能のキーワード: photoprotein, obelin, bioluminescence, atomic resolution, calcium binding, ef-hand, 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: 22943.42

構造登録者

Liu, Z.J.,Vysotski, E.S.,Deng, L.,Lee, J.,Rose, J.,Wang, B.C. (登録日: 2003-08-26, 公開日: 2003-11-11, 最終更新日: 2023-08-16)

主引用文献

Liu, Z.J.,Vysotski, E.S.,Deng, L.,Lee, J.,Rose, J.,Wang, B.C.
Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine.
Biochem.Biophys.Res.Commun., 311:433-439, 2003

PubMed Abstract: The spatial structure of the Ca(2+)-regulated photoprotein obelin has been solved to resolution of 1.1A. Two oxygen atoms are revealed substituted at the C2-position of the coelenterazine in contrast to the obelin structure at 1.73A resolution where one oxygen atom only was disclosed. The electron density of the second oxygen atom was very weak but after exposing the crystals to a trace of Ca(2+), the electron densities of both oxygen atoms became equally intense. In addition, one Ca(2+) was found bound in the loop of the first EF-hand motif. Four of the ligands were provided by protein residues Asp30, Asn32, Asn34, and the main chain oxygen of Lys36. The other two were from water molecules. From a comparison of B-factors for the residues constituting the active site, it is suggested that the variable electron densities observed in various photoprotein structures could be attributed to different mobilities of the peroxy oxygen atoms.

PubMed: 14592432
DOI: 10.1016/j.bbrc.2003.09.231

実験手法

X-RAY DIFFRACTION (1.1 Å)