This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

6pmg

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Solution structure of the C-terminal zinc finger of the C. elegans protein MEX-5

Structural highlights

6pmg is a 1 chain structure with sequence from Caenorhabditis elegans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schubert CM, Lin R, de Vries CJ, Plasterk RH, Priess JR. MEX-5 and MEX-6 function to establish soma/germline asymmetry in early C. elegans embryos. Mol Cell. 2000 Apr;5(4):671-82. PMID:10882103
↑ Nishi Y, Rogers E, Robertson SM, Lin R. Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-primed MEX-5 and MEX-6. Development. 2008 Feb;135(4):687-97. doi: 10.1242/dev.013425. Epub 2008 Jan 16. PMID:18199581 doi:http://dx.doi.org/10.1242/dev.013425
↑ Tenlen JR, Molk JN, London N, Page BD, Priess JR. MEX-5 asymmetry in one-cell C. elegans embryos requires PAR-4- and PAR-1-dependent phosphorylation. Development. 2008 Nov;135(22):3665-75. doi: 10.1242/dev.027060. Epub 2008 Oct 8. PMID:18842813 doi:http://dx.doi.org/10.1242/dev.027060
↑ Saha S, Weber CA, Nousch M, Adame-Arana O, Hoege C, Hein MY, Osborne-Nishimura E, Mahamid J, Jahnel M, Jawerth L, Pozniakovski A, Eckmann CR, Julicher F, Hyman AA. Polar Positioning of Phase-Separated Liquid Compartments in Cells Regulated by an mRNA Competition Mechanism. Cell. 2016 Sep 8;166(6):1572-1584.e16. doi: 10.1016/j.cell.2016.08.006. Epub 2016, Sep 1. PMID:27594427 doi:http://dx.doi.org/10.1016/j.cell.2016.08.006
↑ Tavella D, Ertekin A, Schaal H, Ryder SP, Massi F. A Disorder-to-Order Transition Mediates RNA Binding of the Caenorhabditis elegans Protein MEX-5. Biophys J. 2020 Apr 21;118(8):2001-2014. doi: 10.1016/j.bpj.2020.02.032. Epub, 2020 Mar 19. PMID:32294479 doi:http://dx.doi.org/10.1016/j.bpj.2020.02.032

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/6pmg"

Categories: Caenorhabditis elegans | Large Structures | Massi F | Tavella D

@@ Line 1: / Line 1: @@
 ==Solution structure of the C-terminal zinc finger of the C. elegans protein MEX-5==
-<StructureSection load='6pmg' size='340' side='right'caption='[[6pmg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6pmg' size='340' side='right'caption='[[6pmg]]' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[6pmg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6PMG FirstGlance]. <br>
 </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'>[https://proteopedia.org/fgij/fg.htm?mol=6pmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pmg OCA], [https://pdbe.org/6pmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pmg RCSB], [https://www.ebi.ac.uk/pdbsum/6pmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pmg ProSAT]</span></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>
 == 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>
+[https://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 ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Caeel]]
+[[Category: Caenorhabditis elegans]]
 [[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]]

6pmg

From Proteopedia

Current revision

Solution structure of the C-terminal zinc finger of the C. elegans protein MEX-5

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox