5CD8

Crystal structure of the NTD of Drosophila Oskar protein

Summary for 5CD8

• Entry DOI: 10.2210/pdb5cd8/pdb
• Related: 5cd7 5cd9
• Descriptor: Maternal effect protein oskar, GLYCEROL (3 entities in total)
• Functional Keywords: 3'-utr, dimerization, rna binding protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 6
• Total formula weight: 62576.50

Authors

Yang, N.,Hu, M.,Yu, Z.,Wang, M.,Lehmann, R.,Xu, R.M. (deposition date: 2015-07-03, release date: 2015-09-02, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.001 Å)