7FIF

Cryo-EM structure of the hedgehog release protein Disp from water bear (Hypsibius dujardini)

7FIF の概要

• エントリーDOI: 10.2210/pdb7fif/pdb
• EMDBエントリー: 31595
• 分子名称: Protein dispatched-like protein 1 (1 entity in total)
• 機能のキーワード: cryo-em, dispatched, hedgehog release, hedgehog signaling, membrane protein, setrol sensing domain, water bear
• 由来する生物種: Hypsibius dujardini (Water bear, Macrobiotus dujardini)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 124943.41

構造登録者

Luo, Y.,Wan, G.,Wang, Q.,Zhao, Y.,Cong, Y.,Li, D. (登録日: 2021-07-31, 公開日: 2021-09-08, 最終更新日: 2024-06-12)

主引用文献

Luo, Y.,Wan, G.,Zhou, X.,Wang, Q.,Zhang, Y.,Bao, J.,Cong, Y.,Zhao, Y.,Li, D.
Architecture of Dispatched, a Transmembrane Protein Responsible for Hedgehog Release.
Front Mol Biosci, 8:701826-701826, 2021

PubMed Abstract: The evolutionarily conserved Hedgehog (Hh) signaling pathway is crucial for programmed cell differentiation and proliferation. Dispatched (Disp) is a 12-transmembrane protein that plays a critical role in the Hedgehog (Hh) signaling pathway by releasing the dually lipidated ligand HhN from the membrane, a prerequisite step to the downstream signaling cascade. In this study, we focus on the Disp from water bear, a primitive animal known as the most indestructible on Earth. Using a zebrafish model, we show that the water bear homolog possesses the function of Disp. We have solved its structure to a 6.5-Å resolution using single-particle cryogenic electron microscopy. Consistent with the evolutional conservation of the pathway, the water bear Disp structure is overall similar to the previously reported structures of the fruit fly and human homologs. Although not revealing much detail at this resolution, the water bear Disp shows a different conformation compared to published structures, suggesting that they represent different functional snapshots.

PubMed: 34557519
DOI: 10.3389/fmolb.2021.701826

実験手法

ELECTRON MICROSCOPY (6.5 Å)