6pmg
From Proteopedia
(Difference between revisions)
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==Solution structure of the C-terminal zinc finger of the C. elegans protein MEX-5== | ==Solution structure of the C-terminal zinc finger of the C. elegans protein MEX-5== | ||
| - | <StructureSection load='6pmg' size='340' side='right'caption='[[6pmg]]' scene=''> | + | <StructureSection load='6pmg' size='340' side='right'caption='[[6pmg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[6pmg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PMG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PMG FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6pmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pmg OCA], [http://pdbe.org/6pmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pmg RCSB], [http://www.ebi.ac.uk/pdbsum/6pmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pmg ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mex-5, W02A2.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6pmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pmg OCA], [http://pdbe.org/6pmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pmg RCSB], [http://www.ebi.ac.uk/pdbsum/6pmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pmg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MEX5_CAEEL MEX5_CAEEL]] Functions with mex-6 to affect embryonic viability, establish soma germline asymmetry in embryos and establish plk-1, pie-1, mex-1, and pos-1 asymmetry in embryos (PubMed:10882103, PubMed:18199581, PubMed:18842813). Also affects formation of intestinal cells (PubMed:10882103). Binds to mRNA in vitro, and inhibits pgl-3-mediated P-granule formation, probably by competing with pgl-3 for binding to mRNA (PubMed:27594427).<ref>PMID:10882103</ref> <ref>PMID:18199581</ref> <ref>PMID:18842813</ref> <ref>PMID:27594427</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CCCH-type tandem zinc finger (TZF) domains are found in many RNA-binding proteins (RBPs) that regulate the essential processes of post-transcriptional gene expression and splicing through direct protein-RNA interactions. In Caenorhabditis elegans, RBPs control the translation, stability, or localization of maternal messenger RNAs required for patterning decisions before zygotic gene activation. MEX-5 (Muscle EXcess) is a C. elegans protein that leads a cascade of RBP localization events that is essential for axis polarization and germline differentiation after fertilization. Here, we report that at room temperature, the CCCH-type TZF domain of MEX-5 contains an unstructured zinc finger that folds upon binding of its RNA target. We have characterized the structure and dynamics of the TZF domain of MEX-5 and designed a variant MEX-5 in which both fingers are fully folded in the absence of RNA. Within the thermal range experienced by C. elegans, the population of the unfolded state of the TZF domain of MEX-5 varies. We observe that the TZF domain becomes less disordered at lower temperatures and more disordered at higher temperatures. However, in the temperature range in which C. elegans is fertile, when MEX-5 needs to be functional, only one of the two zinc fingers is folded. | ||
| + | |||
| + | A Disorder-to-Order Transition Mediates RNA Binding of the Caenorhabditis elegans Protein MEX-5.,Tavella D, Ertekin A, Schaal H, Ryder SP, Massi F Biophys J. 2020 Apr 21;118(8):2001-2014. doi: 10.1016/j.bpj.2020.02.032. Epub, 2020 Mar 19. PMID:32294479<ref>PMID:32294479</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6pmg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Caeel]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Massi F]] | + | [[Category: Massi, F]] |
| - | [[Category: Tavella D]] | + | [[Category: Tavella, D]] |
| + | [[Category: C. elegan]] | ||
| + | [[Category: Ccch zinc finger]] | ||
| + | [[Category: Mex-5]] | ||
| + | [[Category: Rna binding protein]] | ||
| + | [[Category: Zinc finger protein]] | ||
Revision as of 06:31, 6 May 2020
Solution structure of the C-terminal zinc finger of the C. elegans protein MEX-5
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