5td6: Difference between revisions
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<StructureSection load='5td6' size='340' side='right'caption='[[5td6]], [[Resolution|resolution]] 2.03Å' scene=''> | <StructureSection load='5td6' size='340' side='right'caption='[[5td6]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5td6]] is a 2 chain structure with sequence from [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.034Å</td></tr> | ||
<tr id=' | <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'>[ | <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> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G5EDX7_CAEEL G5EDX7_CAEEL] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caenorhabditis elegans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Aoki | [[Category: Aoki ST]] | ||
[[Category: Bingman | [[Category: Bingman CA]] | ||
[[Category: Kimble | [[Category: Kimble JE]] | ||
[[Category: Wickens | [[Category: Wickens M]] | ||
Latest revision as of 15:58, 4 October 2023
C. elegans FOG-3 BTG/Tob domain - H47N, C117AC. elegans FOG-3 BTG/Tob domain - H47N, C117A
Structural highlights
FunctionPublication Abstract from PubMedFOG-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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