5td6: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5td6 is ON HOLD
+==C. elegans FOG-3 BTG/Tob domain - H47N, C117A==
+<StructureSection load='5td6' size='340' side='right'caption='[[5td6]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5td6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TD6 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]] 2.034&#8491;</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=5td6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5td6 OCA], [https://pdbe.org/5td6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5td6 RCSB], [https://www.ebi.ac.uk/pdbsum/5td6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5td6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/G5EDX7_CAEEL G5EDX7_CAEEL]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+FOG-3 is a master regulator of sperm fate in Caenorhabditis elegans and homologous to Tob/BTG proteins, which in mammals are monomeric adaptors that recruit enzymes to RNA binding proteins. Here, we determine the FOG-3 crystal structure and in vitro demonstrate that FOG-3 forms dimers that can multimerize. The FOG-3 multimeric structure has a basic surface potential, suggestive of binding nucleic acid. Consistent with that prediction, FOG-3 binds directly to nearly 1,000 RNAs in nematode spermatogenic germ cells. Most binding is to the 3' UTR, and most targets (94%) are oogenic mRNAs, even though assayed in spermatogenic cells. When tethered to a reporter mRNA, FOG-3 represses its expression. Together these findings elucidate the molecular mechanism of sperm fate specification and reveal the evolution of a protein from monomeric to multimeric form with acquisition of a distinct mode of mRNA repression.
-Authors: Aoki, S.T., Bingman, C.A., Wickens, M., Kimble, J.E.
+An RNA-Binding Multimer Specifies Nematode Sperm Fate.,Aoki ST, Porter DF, Prasad A, Wickens M, Bingman CA, Kimble J Cell Rep. 2018 Jun 26;23(13):3769-3775. doi: 10.1016/j.celrep.2018.05.095. PMID:29949762<ref>PMID:29949762</ref>
-Description: C. elegans FOG-3 BTG/Tob domain -H47N, C117A
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Kimble, J.E]]
+<div class="pdbe-citations 5td6" style="background-color:#fffaf0;"></div>
-[[Category: Bingman, C.A]]
+== References ==
-[[Category: Wickens, M]]
+<references/>
-[[Category: Aoki, S.T]]
+__TOC__
+</StructureSection>
+[[Category: Caenorhabditis elegans]]
+[[Category: Large Structures]]
+[[Category: Aoki ST]]
+[[Category: Bingman CA]]
+[[Category: Kimble JE]]
+[[Category: Wickens M]]