2ZBD

Crystal Structure of the SR Calcium Pump with Bound Aluminium Fluoride, ADP and Calcium

「2Z9R」から置き換えられました 「1WPE」から置き換えられました

2ZBD の概要

• エントリーDOI: 10.2210/pdb2zbd/pdb
• 関連するPDBエントリー: 1IWO 1SU4 1VFP 1WPG 2AGV 2DQS 2EAR 2EAS 2EAT 2EAU
• 分子名称: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, CALCIUM ION, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: membrane protein, p-type atpase, had fold, alternative splicing, atp-binding, calcium, calcium transport, endoplasmic reticulum, hydrolase, ion transport, magnesium, metal-binding, nucleotide-binding, phosphorylation, sarcoplasmic reticulum, transmembrane, transport
• 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: 1
• 化学式量合計: 111867.85

構造登録者

Toyoshima, C.,Nomura, H.,Tsuda, T.,Ogawa, H.,Norimatsu, Y. (登録日: 2007-10-20, 公開日: 2007-11-20, 最終更新日: 2024-11-13)

主引用文献

Toyoshima, C.,Nomura, H.,Tsuda, T.
Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
Nature, 432:361-368, 2004

PubMed Abstract: P-type ion transporting ATPases are ATP-powered ion pumps that establish ion concentration gradients across biological membranes. Transfer of bound cations to the lumenal or extracellular side occurs while the ATPase is phosphorylated. Here we report at 2.3 A resolution the structure of the calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative P-type ATPase that is crystallized in the absence of Ca2+ but in the presence of magnesium fluoride, a stable phosphate analogue. This and other crystal structures determined previously provide atomic models for all four principal states in the reaction cycle. These structures show that the three cytoplasmic domains rearrange to move six out of ten transmembrane helices, thereby changing the affinity of the Ca2+-binding sites and the gating of the ion pathway. Release of ADP triggers the opening of the lumenal gate and release of phosphate its closure, effected mainly through movement of the A-domain, the actuator of transmembrane gates.

PubMed: 15448704
DOI: 10.1038/nature02981

実験手法

X-RAY DIFFRACTION (2.4 Å)