5CFF

Crystal structure of Miranda/Staufen dsRBD5 complex

Summary for 5CFF

• Entry DOI: 10.2210/pdb5cff/pdb
• Descriptor: Miranda, Staufen (3 entities in total)
• Functional Keywords: coiled-coil and dsrna-binding domain complex, transcription-rna binding protein complex, transcription/rna binding protein
• Biological source: Drosophila melanogaster (Fruit fly); More
• Total number of polymer chains: 8
• Total formula weight: 74697.62

Authors

Shan, Z.,Wen, W. (deposition date: 2015-07-08, release date: 2015-10-21, Last modification date: 2024-10-23)

Primary citation

Jia, M.,Shan, Z.,Yang, Y.,Liu, C.,Li, J.,Luo, Z.G.,Zhang, M.,Cai, Y.,Wen, W.,Wang, W.
The structural basis of Miranda-mediated Staufen localization during Drosophila neuroblast asymmetric division
Nat Commun, 6:8381-8381, 2015

PubMed Abstract: During the asymmetric division of Drosophila neuroblasts (NBs), the scaffold Miranda (Mira) coordinates the subcellular distribution of cell-fate determinants including Staufen (Stau) and segregates them into the ganglion mother cells (GMCs). Here we show the fifth double-stranded RNA (dsRNA)-binding domain (dsRBD5) of Stau is necessary and sufficient for binding to a coiled-coil region of Mira cargo-binding domain (CBD). The crystal structure of Mira514-595/Stau dsRBD5 complex illustrates that Mira forms an elongated parallel coiled-coil dimer, and two dsRBD5 symmetrically bind to the Mira dimer through their exposed β-sheet faces, revealing a previously unrecognized protein interaction mode for dsRBDs. We further demonstrate that the Mira-Stau dsRBD5 interaction is responsible for the asymmetric localization of Stau during Drosophila NB asymmetric divisions. Finally, we find the CBD-mediated dimer assembly is likely a common requirement for Mira to recognize and translocate other cargos including brain tumour (Brat).

PubMed: 26423004
DOI: 10.1038/ncomms9381

Experimental method

X-RAY DIFFRACTION (2.5 Å)