7S02

Crystal structure of FBF-2 in complex with LST-1 site A peptide and FBE RNA

7S02 の概要

• エントリーDOI: 10.2210/pdb7s02/pdb
• 関連するPDBエントリー: 7RZZ
• 分子名称: Fem-3 mRNA-binding factor 2, FBE RNA, Lateral Signaling Target, ... (6 entities in total)
• 機能のキーワード: pumilio rna-binding proteins, rna binding protein
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 53984.47

構造登録者

Qiu, C.,Hall, T.M.T. (登録日: 2021-08-28, 公開日: 2021-12-29, 最終更新日: 2023-10-18)

主引用文献

Qiu, C.,Wine, R.N.,Campbell, Z.T.,Hall, T.M.T.
Bipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal.
Nucleic Acids Res., 50:536-548, 2022

PubMed Abstract: In C. elegans, PUF proteins promote germline stem cell self-renewal. Their functions hinge on partnerships with two proteins that are redundantly required for stem cell maintenance. Here we focus on understanding how the essential partner protein, LST-1, modulates mRNA regulation by the PUF protein, FBF-2. LST-1 contains two nonidentical sites of interaction with FBF-2, LST-1 A and B. Our crystal structures of complexes of FBF-2, LST-1 A, and RNA visualize how FBF-2 associates with LST-1 A versus LST-1 B. One commonality is that FBF-2 contacts the conserved lysine and leucine side chains in the KxxL motifs in LST-1 A and B. A key difference is that FBF-2 forms unique contacts with regions N- and C-terminal to the KxxL motif. Consequently, LST-1 A does not modulate the RNA-binding affinity of FBF-2, whereas LST-1 B decreases RNA-binding affinity of FBF-2. The N-terminal region of LST-1 B, which binds near the 5' end of RNA elements, is essential to modulate FBF-2 RNA-binding affinity, while the C-terminal residues of LST-1 B contribute strong binding affinity to FBF-2. We conclude that LST-1 has the potential to impact which mRNAs are regulated depending on the precise nature of engagement through its functionally distinct FBF binding sites.

PubMed: 34908132
DOI: 10.1093/nar/gkab1220

実験手法

X-RAY DIFFRACTION (2.34 Å)