3qg9

crystal structure of FBF-2/gld-1 FBEa A7U mutant complex

spinqualitylabelsall models 3qg9, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qg9 is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FBF2_CAEEL Involved in the control of stem cells and sex determination in the C.elegans hermaphrodite germline. May also play a role in the hermaphrodite germline proliferation and oogenesis. Binds specifically to the regulatory region of fem-3 3'-UTR and mediates the sperm/oocyte switch. Negatively regulates gld-3 expression possibly by directly binding to two sites within the gld-3 isoform B 3'-UTR. Publication Abstract from PubMed Stacking interactions between amino acids and bases are common in RNA-protein interactions. Many proteins that regulate mRNAs interact with single-stranded RNA elements in the 3' UTR (3'-untranslated region) of their targets. PUF proteins are exemplary. Here we focus on complexes formed between a Caenorhabditis elegans PUF protein, FBF, and its cognate RNAs. Stacking interactions are particularly prominent and involve every RNA base in the recognition element. To assess the contribution of stacking interactions to formation of the RNA-protein complex, we combine in vivo selection experiments with site-directed mutagenesis, biochemistry, and structural analysis. Our results reveal that the identities of stacking amino acids in FBF affect both the affinity and specificity of the RNA-protein interaction. Substitutions in amino acid side chains can restrict or broaden RNA specificity. We conclude that the identities of stacking residues are important in achieving the natural specificities of PUF proteins. Similarly, in PUF proteins engineered to bind new RNA sequences, the identity of stacking residues may contribute to "target" versus "off-target" interactions, and thus be an important consideration in the design of proteins with new specificities. Stacking interactions in PUF-RNA complexes.,Koh YY, Wang Y, Qiu C, Opperman L, Gross L, Tanaka Hall TM, Wickens M RNA. 2011 Apr;17(4):718-27. Epub 2011 Mar 3. PMID:21372189 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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