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5a48

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Revision as of 16:06, 17 May 2017

Crystal structure of the LOTUS domain (aa 139-240) of Drosophila Oskar in P65

Structural highlights

5a48 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5a49, 5a4a
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5a48"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the LOTUS domain (aa 139-240) of Drosophila Oskar in P65==
 <StructureSection load='5a48' size='340' side='right' caption='[[5a48]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[5a48]] is a 2 chain structure. 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>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a49|5a49]], [[5a4a|5a4a]]</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://www.rcsb.org/pdb/explore.do?structureId=5a48 RCSB], [http://www.ebi.ac.uk/pdbsum/5a48 PDBsum]</span></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>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 5a48" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

5a48

From Proteopedia

Revision as of 16:06, 17 May 2017

Crystal structure of the LOTUS domain (aa 139-240) of Drosophila Oskar in P65

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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