7FIF

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

Summary for 7FIF

• Entry DOI: 10.2210/pdb7fif/pdb
• EMDB information: 31595
• Descriptor: Protein dispatched-like protein 1 (1 entity in total)
• Functional Keywords: cryo-em, dispatched, hedgehog release, hedgehog signaling, membrane protein, setrol sensing domain, water bear
• Biological source: Hypsibius dujardini (Water bear, Macrobiotus dujardini)
• Total number of polymer chains: 1
• Total formula weight: 124943.41

Authors

Luo, Y.,Wan, G.,Wang, Q.,Zhao, Y.,Cong, Y.,Li, D. (deposition date: 2021-07-31, release date: 2021-09-08, Last modification date: 2024-06-12)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (6.5 Å)