6pmg

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

spinqualitylabelsall models 6pmg Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: ZN 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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA