4M59
Crystal structure of the pentatricopeptide repeat protein PPR10 in complex with an 18-nt psaJ RNA element
4M59 の概要
| エントリーDOI | 10.2210/pdb4m59/pdb |
| 関連するPDBエントリー | 4M57 |
| 分子名称 | Chloroplast pentatricopeptide repeat protein 10, psaJ RNA, PHOSPHATE ION, ... (4 entities in total) |
| 機能のキーワード | pentatricopeptide repeats, superhelical, rna binding protein, rna, rna binding protein-rna complex, rna binding protein/rna |
| 由来する生物種 | Zea mays (maize) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 169856.71 |
| 構造登録者 | |
| 主引用文献 | Yin, P.,Li, Q.,Yan, C.,Liu, Y.,Liu, J.,Yu, F.,Wang, Z.,Long, J.,He, J.,Wang, H.W.,Wang, J.,Zhu, J.K.,Shi, Y.,Yan, N. Structural basis for the modular recognition of single-stranded RNA by PPR proteins. Nature, 504:168-171, 2013 Cited by PubMed Abstract: Pentatricopeptide repeat (PPR) proteins represent a large family of sequence-specific RNA-binding proteins that are involved in multiple aspects of RNA metabolism. PPR proteins, which are found in exceptionally large numbers in the mitochondria and chloroplasts of terrestrial plants, recognize single-stranded RNA (ssRNA) in a modular fashion. The maize chloroplast protein PPR10 binds to two similar RNA sequences from the ATPI-ATPH and PSAJ-RPL33 intergenic regions, referred to as ATPH and PSAJ, respectively. By protecting the target RNA elements from 5' or 3' exonucleases, PPR10 defines the corresponding 5' and 3' messenger RNA termini. Despite rigorous functional characterizations, the structural basis of sequence-specific ssRNA recognition by PPR proteins remains to be elucidated. Here we report the crystal structures of PPR10 in RNA-free and RNA-bound states at resolutions of 2.85 and 2.45 Å, respectively. In the absence of RNA binding, the nineteen repeats of PPR10 are assembled into a right-handed superhelical spiral. PPR10 forms an antiparallel, intertwined homodimer and exhibits considerable conformational changes upon binding to its target ssRNA, an 18-nucleotide PSAJ element. Six nucleotides of PSAJ are specifically recognized by six corresponding PPR10 repeats following the predicted code. The molecular basis for the specific and modular recognition of RNA bases A, G and U is revealed. The structural elucidation of RNA recognition by PPR proteins provides an important framework for potential biotechnological applications of PPR proteins in RNA-related research areas. PubMed: 24162847DOI: 10.1038/nature12651 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.46 Å) |
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