5BYM

Crystal structure of the RNA-binding domain of yeast Puf5p bound to SMX2 RNA

5BYM の概要

• エントリーDOI: 10.2210/pdb5bym/pdb
• 関連するPDBエントリー: 5BZ1 5BZ5
• 分子名称: Suppressor protein MPT5, RNA (5'-R(*UP*GP*UP*AP*CP*UP*AP*UP*A)-3') (2 entities in total)
• 機能のキーワード: puf rna-binding domain, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm : P39016
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48128.13

構造登録者

Qiu, C.,Hall, T.M.T. (登録日: 2015-06-10, 公開日: 2015-09-23, 最終更新日: 2024-03-06)

主引用文献

Wilinski, D.,Qiu, C.,Lapointe, C.P.,Nevil, M.,Campbell, Z.T.,Tanaka Hall, T.M.,Wickens, M.
RNA regulatory networks diversified through curvature of the PUF protein scaffold.
Nat Commun, 6:8213-8213, 2015

PubMed Abstract: 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.

PubMed: 26364903
DOI: 10.1038/ncomms9213

実験手法

X-RAY DIFFRACTION (2.708 Å)