5A48
Crystal structure of the LOTUS domain (aa 139-240) of Drosophila Oskar in P65
Summary for 5A48
| Entry DOI | 10.2210/pdb5a48/pdb |
| Related | 5A49 5A4A |
| Descriptor | MATERNAL EFFECT PROTEIN OSKAR (2 entities in total) |
| Functional Keywords | protein binding, ost-hth domain, winged helix-turn-helix, dimer, vasa interaction, germ plasm |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 2 |
| Total formula weight | 23402.47 |
| Authors | Jeske, M.,Glatt, S.,Ephrussi, A.,Mueller, C.W. (deposition date: 2015-06-05, release date: 2015-07-22, Last modification date: 2024-05-08) |
| Primary citation | Jeske, M.,Bordi, M.,Glatt, S.,Muller, S.,Rybin, V.,Muller, C.W.,Ephrussi, A. The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase-and RNA-Binding Activities. Cell Rep., 12:587-, 2015 Cited by PubMed Abstract: In many animals, the germ plasm segregates germline from soma during early development. Oskar protein is known for its ability to induce germ plasm formation and germ cells in Drosophila. However, the molecular basis of germ plasm formation remains unclear. Here, we show that Oskar is an RNA-binding protein in vivo, crosslinking to nanos, polar granule component, and germ cell-less mRNAs, each of which has a role in germline formation. Furthermore, we present high-resolution crystal structures of the two Oskar domains. RNA-binding maps in vitro to the C-terminal domain, which shows structural similarity to SGNH hydrolases. The highly conserved N-terminal LOTUS domain forms dimers and mediates Oskar interaction with the germline-specific RNA helicase Vasa in vitro. Our findings suggest a dual function of Oskar in RNA and Vasa binding, providing molecular clues to its germ plasm function. PubMed: 26190108DOI: 10.1016/J.CELREP.2015.06.055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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