6PUN

Crystal structure of a ternary complex of FBF-2 with LST-1 (site B) and compact FBE RNA

6PUN の概要

• エントリーDOI: 10.2210/pdb6pun/pdb
• 分子名称: Fem-3 mRNA-binding factor 2, RNA (5'-R(*CP*UP*GP*UP*GP*AP*AP*U)-3'), LST-1, ... (7 entities in total)
• 機能のキーワード: puf, protein-rna complex, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 106096.28

構造登録者

Qiu, C.,Campbell, Z.T.,Hall, T.M.T. (登録日: 2019-07-18, 公開日: 2019-08-21, 最終更新日: 2023-10-11)

主引用文献

Qiu, C.,Bhat, V.D.,Rajeev, S.,Zhang, C.,Lasley, A.E.,Wine, R.N.,Campbell, Z.T.,Tanaka Hall, T.M.T.
A crystal structure of a collaborative RNA regulatory complex reveals mechanisms to refine target specificity.
Elife, 8:-, 2019

PubMed Abstract: In the germline, Binding Factor (FBF) partners with LST-1 to maintain stem cells. A crystal structure of an FBF-2/LST-1/RNA complex revealed that FBF-2 recognizes a short RNA motif different from the characteristic 9-nt FBF binding element, and compact motif recognition coincided with curvature changes in the FBF-2 scaffold. Previously, we engineered FBF-2 to favor recognition of shorter RNA motifs without curvature change (Bhat et al., 2019). In vitro selection of RNAs bound by FBF-2 suggested sequence specificity in the central region of the compact element. This bias, reflected in the crystal structure, was validated in RNA-binding assays. FBF-2 has the intrinsic ability to bind to this shorter motif. LST-1 weakens FBF-2 binding affinity for short and long motifs, which may increase target selectivity. Our findings highlight the role of FBF scaffold flexibility in RNA recognition and suggest a new mechanism by which protein partners refine target site selection.

PubMed: 31397673
DOI: 10.7554/eLife.48968

実験手法

X-RAY DIFFRACTION (2.099 Å)