5a4a
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5a4a is ON HOLD until Paper Publication Authors: Jeske, M., Glatt, S., Ephrussi, A., Mueller, C.W. Description: Crystal structure of the OSK domain...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the OSK domain of Drosophila Oskar== | |
| + | <StructureSection load='5a4a' size='340' side='right'caption='[[5a4a]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5a4a]] is a 1 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=5A4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A4A FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.699Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5a4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a4a OCA], [https://pdbe.org/5a4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a4a RCSB], [https://www.ebi.ac.uk/pdbsum/5a4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a4a ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == 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<ref>PMID:26190108</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5a4a" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ephrussi A]] | ||
| + | [[Category: Glatt S]] | ||
| + | [[Category: Jeske M]] | ||
| + | [[Category: Mueller CW]] | ||
Current revision
Crystal structure of the OSK domain of Drosophila Oskar
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