5bzu

Crystal structure of the RNA-binding domain of yeast Puf5p bound to AAT2 RNA

spinqualitylabelsall models 5bzu, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5bzu is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MPT5_YEAST RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of HO by binding to the 3'-UTR of HO mRNA. Predominantly binds to mRNAs encoding chromatin modifiers and spindle pole body components. Recognizes and binds to 5'-TGTAA[CT]A[AT]TA-3' in the 3'-UTR of target mRNAs. Multicopy suppressor of POP2 mutation. Required for high temperature growth. Publication Abstract from PubMed Proteins bind and control mRNAs, directing their localization, translation and stability. Members of the PUF family of RNA-binding proteins control multiple mRNAs in a single cell, and play key roles in development, stem cell maintenance and memory formation. Here we identified the mRNA targets of a S. cerevisiae PUF protein, Puf5p, by ultraviolet-crosslinking-affinity purification and high-throughput sequencing (HITS-CLIP). The binding sites recognized by Puf5p are diverse, with variable spacer lengths between two specific sequences. Each length of site correlates with a distinct biological function. Crystal structures of Puf5p-RNA complexes reveal that the protein scaffold presents an exceptionally flat and extended interaction surface relative to other PUF proteins. In complexes with RNAs of different lengths, the protein is unchanged. A single PUF protein repeat is sufficient to induce broadening of specificity. Changes in protein architecture, such as alterations in curvature, may lead to evolution of mRNA regulatory networks. RNA regulatory networks diversified through curvature of the PUF protein scaffold.,Wilinski D, Qiu C, Lapointe CP, Nevil M, Campbell ZT, Tanaka Hall TM, Wickens M Nat Commun. 2015 Sep 14;6:8213. doi: 10.1038/ncomms9213. PMID:26364903 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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