5a49: Difference between revisions

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 ==Crystal structure of the LOTUS domain (aa 139-222) of Drosophila Oskar in C222==
-<StructureSection load='5a49' size='340' side='right' caption='[[5a49]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='5a49' size='340' side='right'caption='[[5a49]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5a49]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A49 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5a49]] is a 10 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=5A49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A49 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a48|5a48]], [[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]] 2.098&#8491;</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=5a49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a49 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a49 RCSB], [http://www.ebi.ac.uk/pdbsum/5a49 PDBsum]</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=5a49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a49 OCA], [https://pdbe.org/5a49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a49 RCSB], [https://www.ebi.ac.uk/pdbsum/5a49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a49 ProSAT]</span></td></tr>
 </table>
 == 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;">
+== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5a49" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ephrussi, A]]
+[[Category: Drosophila melanogaster]]
-[[Category: Glatt, S]]
+[[Category: Large Structures]]
-[[Category: Jeske, M]]
+[[Category: Ephrussi A]]
-[[Category: Mueller, C W]]
+[[Category: Glatt S]]
-[[Category: Dimer]]
+[[Category: Jeske M]]
-[[Category: Germ plasm]]
+[[Category: Mueller CW]]
-[[Category: Ost-hth domain]]
-[[Category: Protein binding]]
-[[Category: Protein binding interaction]]
-[[Category: Vasa]]
-[[Category: Winged helix-turn-helix]]