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| | <StructureSection load='5a48' size='340' side='right'caption='[[5a48]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5a48' size='340' side='right'caption='[[5a48]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a48]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A48 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a48]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A48 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a49|5a49]], [[5a4a|5a4a]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a48 OCA], [http://pdbe.org/5a48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a48 RCSB], [http://www.ebi.ac.uk/pdbsum/5a48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a48 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a48 OCA], [https://pdbe.org/5a48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a48 RCSB], [https://www.ebi.ac.uk/pdbsum/5a48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a48 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OSKA_DROME OSKA_DROME]] Organizes the germ plasm and directs localization of the posterior determinant nanos. Oskar protein is required to keep nos RNA and staufen protein at the posterior pole.<ref>PMID:1641021</ref> <ref>PMID:2070416</ref> <ref>PMID:2070417</ref> | + | [https://www.uniprot.org/uniprot/OSKA_DROME OSKA_DROME] Organizes the germ plasm and directs localization of the posterior determinant nanos. Oskar protein is required to keep nos RNA and staufen protein at the posterior pole.<ref>PMID:1641021</ref> <ref>PMID:2070416</ref> <ref>PMID:2070417</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ephrussi, A]] | + | [[Category: Ephrussi A]] |
| - | [[Category: Glatt, S]] | + | [[Category: Glatt S]] |
| - | [[Category: Jeske, M]] | + | [[Category: Jeske M]] |
| - | [[Category: Mueller, C W]] | + | [[Category: Mueller CW]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Germ plasm]]
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| - | [[Category: Ost-hth domain]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Vasa interaction]]
| + | |
| - | [[Category: Winged helix-turn-helix]]
| + | |
| Structural highlights
Function
OSKA_DROME Organizes the germ plasm and directs localization of the posterior determinant nanos. Oskar protein is required to keep nos RNA and staufen protein at the posterior pole.[1] [2] [3]
Publication Abstract from PubMed
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.
The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities.,Jeske M, Bordi M, Glatt S, Muller S, Rybin V, Muller CW, Ephrussi A Cell Rep. 2015 Jul 15. pii: S2211-1247(15)00681-6. doi:, 10.1016/j.celrep.2015.06.055. PMID:26190108[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ephrussi A, Lehmann R. Induction of germ cell formation by oskar. Nature. 1992 Jul 30;358(6385):387-92. PMID:1641021 doi:http://dx.doi.org/10.1038/358387a0
- ↑ Kim-Ha J, Smith JL, Macdonald PM. oskar mRNA is localized to the posterior pole of the Drosophila oocyte. Cell. 1991 Jul 12;66(1):23-35. PMID:2070416
- ↑ Ephrussi A, Dickinson LK, Lehmann R. Oskar organizes the germ plasm and directs localization of the posterior determinant nanos. Cell. 1991 Jul 12;66(1):37-50. PMID:2070417
- ↑ Jeske M, Bordi M, Glatt S, Muller S, Rybin V, Muller CW, Ephrussi A. The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities. Cell Rep. 2015 Jul 15. pii: S2211-1247(15)00681-6. doi:, 10.1016/j.celrep.2015.06.055. PMID:26190108 doi:http://dx.doi.org/10.1016/j.celrep.2015.06.055
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