5CD9

Crystal structure of the CTD of Drosophila Oskar protein

5CD9 の概要

• エントリーDOI: 10.2210/pdb5cd9/pdb
• 関連するPDBエントリー: 5cd7 5cd8
• 分子名称: Maternal effect protein oskar, SULFATE ION (3 entities in total)
• 機能のキーワード: 3'-utr, dimerization, rna binding protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25975.90

構造登録者

Yang, N.,Hu, M.,Yu, Z.,Wang, M.,Lehmann, R.,Xu, R.M. (登録日: 2015-07-03, 公開日: 2015-09-02, 最終更新日: 2024-10-23)

主引用文献

Yang, N.,Yu, Z.,Hu, M.,Wang, M.,Lehmann, R.,Xu, R.M.
Structure of Drosophila Oskar reveals a novel RNA binding protein
Proc.Natl.Acad.Sci.USA, 112:11541-11546, 2015

PubMed Abstract: Oskar (Osk) protein plays critical roles during Drosophila germ cell development, yet its functions in germ-line formation and body patterning remain poorly understood. This situation contrasts sharply with the vast knowledge about the function and mechanism of osk mRNA localization. Osk is predicted to have an N-terminal LOTUS domain (Osk-N), which has been suggested to bind RNA, and a C-terminal hydrolase-like domain (Osk-C) of unknown function. Here, we report the crystal structures of Osk-N and Osk-C. Osk-N shows a homodimer of winged-helix-fold modules, but without detectable RNA-binding activity. Osk-C has a lipase-fold structure but lacks critical catalytic residues at the putative active site. Surprisingly, we found that Osk-C binds the 3'UTRs of osk and nanos mRNA in vitro. Mutational studies identified a region of Osk-C important for mRNA binding. These results suggest possible functions of Osk in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3'UTRs, and provide structural insights into a novel protein-RNA interaction motif involving a hydrolase-related domain.

PubMed: 26324911
DOI: 10.1073/pnas.1515568112

実験手法

X-RAY DIFFRACTION (2.102 Å)