2ZBE

Calcium pump crystal structure with bound BeF3 in the absence of calcium and TG

2ZBE の概要

• エントリーDOI: 10.2210/pdb2zbe/pdb
• 関連するPDBエントリー: 1IWO 1SU4 1VFP 1WPG 2AGV 2DQS 2EAR 2EAS 2EAT 2EAU 2ZBD 2ZBF 2ZBG
• 分子名称: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION (3 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: 2
• 化学式量合計: 219437.86

構造登録者

Toyoshima, C.,Ogawa, H.,Norimatsu, Y. (登録日: 2007-10-20, 公開日: 2007-12-11, 最終更新日: 2023-11-01)

主引用文献

Toyoshima, C.,Norimatsu, Y.,Iwasawa, S.,Tsuda, T.,Ogawa, H.
How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump
Proc.Natl.Acad.Sci.Usa, 104:19831-19836, 2007

PubMed Abstract: Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum is the best-studied member of the P-type or E1/E2 type ion transporting ATPases. It has been crystallized in seven different states that cover nearly the entire reaction cycle. Here we describe the structure of this ATPase complexed with phosphate analogs BeF(3)(-) and AlF(4)(-) in the absence of Ca(2+), which correspond to the E2P ground state and E2 approximately P transition state, respectively. The luminal gate is open with BeF(3)(-) and closed with AlF(4)(-). These and the E1 approximately P.ADP analog crystal structures show that a two-step rotation of the cytoplasmic A-domain opens and closes the luminal gate through the movements of the M1-M4 transmembrane helices. There are several conformational switches coupled to the rotation, and the one in the cytoplasmic part of M2 has critical importance. In the second step of rotation, positioning of one water molecule couples the hydrolysis of aspartylphosphate to closing of the gate.

PubMed: 18077416
DOI: 10.1073/pnas.0709978104

実験手法

X-RAY DIFFRACTION (3.8 Å)