1VFP

Crystal structure of the SR CA2+-ATPase with bound AMPPCP

1VFP の概要

• エントリーDOI: 10.2210/pdb1vfp/pdb
• 関連するPDBエントリー: 1IWO 1SU4
• 分子名称: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: membrane protein, p-type atpase, had fold, hydrolase
• 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: 220424.49

構造登録者

Toyoshima, C.,Mizutani, T. (登録日: 2004-04-18, 公開日: 2004-07-06, 最終更新日: 2024-11-20)

主引用文献

Toyoshima, C.,Mizutani, T.
Crystal structure of the calcium pump with a bound ATP analogue.
Nature, 430:529-535, 2004

PubMed Abstract: P-type ATPases are ATP-powered ion pumps that establish ion concentration gradients across cell and organelle membranes. Here, we describe the crystal structure of the Ca2+ pump of skeletal muscle sarcoplasmic reticulum, a representative member of the P-type ATPase superfamily, with an ATP analogue, a Mg2+ and two Ca2+ ions in the respective binding sites. In this state, the ATP analogue reorganizes the three cytoplasmic domains (A, N and P), which are widely separated without nucleotide, by directly bridging the N and P domains. The structure of the P-domain itself is altered by the binding of the ATP analogue and Mg2+. As a result, the A-domain is tilted so that one of the transmembrane helices moves to lock the cytoplasmic gate of the transmembrane Ca2+-binding sites. This appears to be the mechanism for occluding the bound Ca2+ ions, before releasing them into the lumen of the sarcoplasmic reticulum.

PubMed: 15229613
DOI: 10.1038/nature02680

実験手法

X-RAY DIFFRACTION (2.9 Å)