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1SL7

Crystal structure of calcium-loaded apo-obelin from Obelia longissima

1SL7 の概要
エントリーDOI10.2210/pdb1sl7/pdb
関連するPDBエントリー1EJ3 1EL4 1JF0 1JF2 1QV0 1QV1 1S36
分子名称Obelin, CALCIUM ION (3 entities in total)
機能のキーワードphotoprotein, obelin, bioluminescence, calcium binding, ef-hand, aequorin, fluorescence, structural genomics, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, 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22376.13
構造登録者
Deng, L.,Markova, S.V.,Vysotski, E.S.,Liu, Z.J.,Lee, J.,Rose, J.,Wang, B.C.,Southeast Collaboratory for Structural Genomics (SECSG) (登録日: 2004-03-05, 公開日: 2004-12-28, 最終更新日: 2023-08-23)
主引用文献Deng, L.,Vysotski, E.S.,Markova, S.V.,Liu, Z.J.,Lee, J.,Rose, J.,Wang, B.C.
All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obelin.
Protein Sci., 14:663-675, 2005
Cited by
PubMed 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.
PubMed: 15689515
DOI: 10.1110/ps.041142905
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 1sl7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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