6TBU

Structure of Drosophila melanogaster Dispatched

Summary for 6TBU

• Entry DOI: 10.2210/pdb6tbu/pdb
• EMDB information: 10452
• Descriptor: Protein dispatched, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHOLESTEROL HEMISUCCINATE, ... (4 entities in total)
• Functional Keywords: rnd transporter, transmembrane domain, ectodomain, cholesteryl hemisuccinate, detergent micelle, digitonin, monomer, membrane protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 144176.02

Authors

Korkhov, V.M.,Cannac, F. (deposition date: 2019-11-04, release date: 2020-06-03, Last modification date: 2020-07-29)

Primary citation

Cannac, F.,Qi, C.,Falschlunger, J.,Hausmann, G.,Basler, K.,Korkhov, V.M.
Cryo-EM structure of the Hedgehog release protein Dispatched.
Sci Adv, 6:eaay7928-eaay7928, 2020

PubMed Abstract: The Hedgehog (Hh) signaling pathway controls embryonic development and adult tissue homeostasis in multicellular organisms. In , the pathway is primed by secretion of a dually lipid-modified morphogen, Hh, a process dependent on a membrane-integral protein Dispatched. Although Dispatched is a critical component of the pathway, the structural basis of its activity has, so far, not been described. Here, we describe a cryo-electron microscopy structure of the Dispatched at 3.2-Å resolution. The ectodomains of Dispatched adopt an open conformation suggestive of a receptor-chaperone role. A three-dimensional reconstruction of Dispatched bound to Hh confirms the ability of Dispatched to bind Hh but using a unique mode distinct from those previously observed in structures of Hh complexes. The structure may represent the state of the complex that precedes shedding of Hh from the surface of the morphogen-releasing cell.

PubMed: 32494603
DOI: 10.1126/sciadv.aay7928

Experimental method

ELECTRON MICROSCOPY (3.16 Å)