5L7Z
Structure of Exuperantia EXO-like domain
Summary for 5L7Z
Entry DOI | 10.2210/pdb5l7z/pdb |
Descriptor | Maternal protein exuperantia (2 entities in total) |
Functional Keywords | exonuclease, rna, pseudo nuclease, hydrolase, rna binding protein |
Biological source | Drosophila melanogaster (Fruit fly) |
Total number of polymer chains | 1 |
Total formula weight | 36628.59 |
Authors | Lazzaretti, D.,Veith, K.,Bono, F. (deposition date: 2016-06-05, release date: 2016-07-06, Last modification date: 2024-05-08) |
Primary citation | Lazzaretti, D.,Veith, K.,Kramer, K.,Basquin, C.,Urlaub, H.,Irion, U.,Bono, F. The bicoid mRNA localization factor Exuperantia is an RNA-binding pseudonuclease. Nat.Struct.Mol.Biol., 23:705-713, 2016 Cited by PubMed Abstract: Anterior patterning in Drosophila is mediated by the localization of bicoid (bcd) mRNA at the anterior pole of the oocyte. Exuperantia (Exu) is a putative exonuclease (EXO) associated with bcd and required for its localization. We present the crystal structure of Exu, which reveals a dimeric assembly with each monomer consisting of a 3'-5' EXO-like domain and a sterile alpha motif (SAM)-like domain. The catalytic site is degenerate and inactive. Instead, the EXO-like domain mediates dimerization and RNA binding. We show that Exu binds RNA directly in vitro, that the SAM-like domain is required for RNA binding activity and that Exu binds a structured element present in the bcd 3' untranslated region with high affinity. Through structure-guided mutagenesis, we show that Exu dimerization is essential for bcd localization. Our data demonstrate that Exu is a noncanonical RNA-binding protein with EXO-SAM-like domain architecture that interacts with its target RNA as a homodimer. PubMed: 27376588DOI: 10.1038/nsmb.3254 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
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