5cd7: Difference between revisions
New page: '''Unreleased structure''' The entry 5cd7 is ON HOLD until Paper Publication Authors: Yang, N., Hu, M., Yu, Z., Wang, M., Lehmann, R., Xu, R.M. Description: Crystal structure of the NT... |
No edit summary |
||
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of the NTD L199M of Drosophila Oskar protein== | |||
<StructureSection load='5cd7' size='340' side='right'caption='[[5cd7]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cd7]] is a 6 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=5CD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CD7 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]] 2.502Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5cd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cd7 OCA], [https://pdbe.org/5cd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cd7 RCSB], [https://www.ebi.ac.uk/pdbsum/5cd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cd7 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 == | |||
Oskar (Osk) protein plays critical roles during Drosophila germ cell development, yet its functions in germ-line formation and body patterning remain poorly understood. This situation contrasts sharply with the vast knowledge about the function and mechanism of osk mRNA localization. Osk is predicted to have an N-terminal LOTUS domain (Osk-N), which has been suggested to bind RNA, and a C-terminal hydrolase-like domain (Osk-C) of unknown function. Here, we report the crystal structures of Osk-N and Osk-C. Osk-N shows a homodimer of winged-helix-fold modules, but without detectable RNA-binding activity. Osk-C has a lipase-fold structure but lacks critical catalytic residues at the putative active site. Surprisingly, we found that Osk-C binds the 3'UTRs of osk and nanos mRNA in vitro. Mutational studies identified a region of Osk-C important for mRNA binding. These results suggest possible functions of Osk in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3'UTRs, and provide structural insights into a novel protein-RNA interaction motif involving a hydrolase-related domain. | |||
Structure of Drosophila Oskar reveals a novel RNA binding protein.,Yang N, Yu Z, Hu M, Wang M, Lehmann R, Xu RM Proc Natl Acad Sci U S A. 2015 Sep 15;112(37):11541-6. doi:, 10.1073/pnas.1515568112. Epub 2015 Aug 31. PMID:26324911<ref>PMID:26324911</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5cd7" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | |||
[[Category: Hu M]] | |||
[[Category: Lehmann R]] | |||
[[Category: Wang M]] | |||
[[Category: Xu RM]] | |||
[[Category: Yang N]] | |||
[[Category: Yu Z]] | |||
Latest revision as of 11:46, 23 October 2024
Crystal structure of the NTD L199M of Drosophila Oskar proteinCrystal structure of the NTD L199M of Drosophila Oskar protein
Structural highlights
FunctionOSKA_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 PubMedOskar (Osk) protein plays critical roles during Drosophila germ cell development, yet its functions in germ-line formation and body patterning remain poorly understood. This situation contrasts sharply with the vast knowledge about the function and mechanism of osk mRNA localization. Osk is predicted to have an N-terminal LOTUS domain (Osk-N), which has been suggested to bind RNA, and a C-terminal hydrolase-like domain (Osk-C) of unknown function. Here, we report the crystal structures of Osk-N and Osk-C. Osk-N shows a homodimer of winged-helix-fold modules, but without detectable RNA-binding activity. Osk-C has a lipase-fold structure but lacks critical catalytic residues at the putative active site. Surprisingly, we found that Osk-C binds the 3'UTRs of osk and nanos mRNA in vitro. Mutational studies identified a region of Osk-C important for mRNA binding. These results suggest possible functions of Osk in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3'UTRs, and provide structural insights into a novel protein-RNA interaction motif involving a hydrolase-related domain. Structure of Drosophila Oskar reveals a novel RNA binding protein.,Yang N, Yu Z, Hu M, Wang M, Lehmann R, Xu RM Proc Natl Acad Sci U S A. 2015 Sep 15;112(37):11541-6. doi:, 10.1073/pnas.1515568112. Epub 2015 Aug 31. PMID:26324911[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||