1IWO

Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+

1IWO の概要

• エントリーDOI: 10.2210/pdb1iwo/pdb
• 関連するPDBエントリー: 1EUL
• 分子名称: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,-3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OX Y]-2-OXO-4-(1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER (2 entities in total)
• 機能のキーワード: membrane protein, p-type atpase, had fold, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Endoplasmic reticulum membrane; Multi-pass membrane protein: P04191
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 220506.66

構造登録者

Toyoshima, C.,Nomura, H. (登録日: 2002-05-26, 公開日: 2002-08-14, 最終更新日: 2024-10-23)

主引用文献

Toyoshima, C.,Nomura, H.
Structural changes in the calcium pump accompanying the dissociation of calcium
Nature, 418:605-611, 2002

PubMed Abstract: In skeletal muscle, calcium ions are transported (pumped) against a concentration gradient from the cytoplasm into the sarcoplasmic reticulum, an intracellular organelle. This causes muscle cells to relax after cytosolic calcium increases during excitation. The Ca(2+) ATPase that carries out this pumping is a representative P-type ion-transporting ATPase. Here we describe the structure of this ion pump at 3.1 A resolution in a Ca(2+)-free (E2) state, and compare it with that determined previously for the Ca(2+)-bound (E1Ca(2+)) state. The structure of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large conformation differences from that in E1Ca(2+). Three cytoplasmic domains gather to form a single headpiece, and six of the ten transmembrane helices exhibit large-scale rearrangements. These rearrangements ensure the release of calcium ions into the lumen of sarcoplasmic reticulum and, on the cytoplasmic side, create a pathway for entry of new calcium ions.

PubMed: 12167852
DOI: 10.1038/nature00944

実験手法

X-RAY DIFFRACTION (3.1 Å)