5XA7

Complete structure factors and an atomic model of the calcium pump (SERCA1A) and associated phospholipids in the E1-2CA2+ crystals

5XA7 の概要

• エントリーDOI: 10.2210/pdb5xa7/pdb
• 関連するPDBエントリー: 5XA8 5XA9 5XAA 5XAB
• 分子名称: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, CALCIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: p-type atpase, hydrolase, calcium transport, calcium binding, endoplasmic reticulum, sarcoplasmic reticulum, met 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: 136493.88

構造登録者

Norimatsu, Y.,Hasegawa, K.,Shimizu, N.,Toyoshima, C. (登録日: 2017-03-11, 公開日: 2017-05-17, 最終更新日: 2024-10-09)

主引用文献

Norimatsu, Y.,Hasegawa, K.,Shimizu, N.,Toyoshima, C.
Protein-phospholipid interplay revealed with crystals of a calcium pump.
Nature, 545:193-198, 2017

PubMed Abstract: The lipid bilayer has so far eluded visualization by conventional crystallographic methods, severely limiting our understanding of phospholipid- and protein-phospholipid interactions. Here we describe electron density maps for crystals of Ca-ATPase in four different states obtained by X-ray solvent contrast modulation. These maps resolve the entire first layer of phospholipids surrounding the transmembrane helices, although less than half of them are hydrogen-bonded to protein residues. Phospholipids follow the movements of associated residues, causing local distortions and changes in thickness of the bilayer. Unexpectedly, the entire protein tilts during the reaction cycle, governed primarily by a belt of Trp residues, to minimize energy costs accompanying the large perpendicular movements of the transmembrane helices. A class of Arg residues extend their side chains through the cytoplasm to exploit phospholipids as anchors for conformational switching. Thus, phospholipid-Arg/Lys and phospholipid-Trp interactions have distinct functional roles in the dynamics of ion pumps and, presumably, membrane proteins in general.

PubMed: 28467821
DOI: 10.1038/nature22357

実験手法

X-RAY DIFFRACTION (3.2 Å)