7P14

Structure of full-length rXKR9 in complex with a sybody at 3.66A

7P14 の概要

• エントリーDOI: 10.2210/pdb7p14/pdb
• EMDBエントリー: 13155
• 分子名称: XK-related protein, Sybody, DIUNDECYL PHOSPHATIDYL CHOLINE, ... (4 entities in total)
• 機能のキーワード: small membrane protein, in complex with sybody, apoptotic lipid scrambling, membrane protein
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59276.09

構造登録者

Straub, M.S.,Sawicka, M.,Dutzler, R. (登録日: 2021-07-01, 公開日: 2021-07-28, 最終更新日: 2024-11-13)

主引用文献

Straub, M.S.,Alvadia, C.,Sawicka, M.,Dutzler, R.
Cryo-EM structures of the caspase activated protein XKR9 involved in apoptotic lipid scrambling.
Elife, 10:-, 2021

PubMed Abstract: The exposure of the negatively charged lipid phosphatidylserine on the cell surface, catalyzed by lipid scramblases, is an important signal for the clearance of apoptotic cells by macrophages. The protein XKR9 is a member of a conserved family that has been associated with apoptotic lipid scrambling. Here, we describe structures of full-length and caspase-treated XKR9 from in complex with a synthetic nanobody determined by cryo-electron microscopy. The 43 kDa monomeric membrane protein can be divided into two structurally related repeats, each containing four membrane-spanning segments and a helix that is partly inserted into the lipid bilayer. In the full-length protein, the C-terminus interacts with a hydrophobic pocket located at the intracellular side acting as an inhibitor of protein function. Cleavage by caspase-3 at a specific site releases 16 residues of the C-terminus, thus making the pocket accessible to the cytoplasm. Collectively, the work has revealed the unknown architecture of the XKR family and has provided initial insight into its activation by caspases.

PubMed: 34263724
DOI: 10.7554/eLife.69800

実験手法

ELECTRON MICROSCOPY (3.66 Å)