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4CYK

Structural basis for binding of Pan3 to Pan2 and its function in mRNA recruitment and deadenylation

4CYK の概要
エントリーDOI10.2210/pdb4cyk/pdb
NMR情報BMRB: 19959
分子名称PAB-DEPENDENT POLY(A)-SPECIFIC RIBONUCLEASE SUBUNIT PAN3, ZINC ION (2 entities in total)
機能のキーワードtranscription, pan3p, pan2p, polya, rna, deadenylation
由来する生物種SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
細胞内の位置Cytoplasm : P36102
タンパク質・核酸の鎖数1
化学式量合計4806.81
構造登録者
主引用文献Wolf, J.,Valkov, E.,Allen, M.D.,Meineke, B.,Gordiyenko, Y.,Mclaughlin, S.H.,Olsen, T.M.,Robinson, C.V.,Bycroft, M.,Stewart, M.,Passmore, L.A.
Structural Basis for Pan3 Binding to Pan2 and its Function in Mrna Recruitment and Deadenylation.
Embo J., 33:1514-, 2014
Cited by
PubMed Abstract: The conserved eukaryotic Pan2-Pan3 deadenylation complex shortens cytoplasmic mRNA 3' polyA tails to regulate mRNA stability. Although the exonuclease activity resides in Pan2, efficient deadenylation requires Pan3. The mechanistic role of Pan3 is unclear. Here, we show that Pan3 binds RNA directly both through its pseudokinase/C-terminal domain and via an N-terminal zinc finger that binds polyA RNA specifically. In contrast, isolated Pan2 is unable to bind RNA. Pan3 binds to the region of Pan2 that links its N-terminal WD40 domain to the C-terminal part that contains the exonuclease, with a 2:1 stoichiometry. The crystal structure of the Pan2 linker region bound to a Pan3 homodimer shows how the unusual structural asymmetry of the Pan3 dimer is used to form an extensive high-affinity interaction. This binding allows Pan3 to supply Pan2 with substrate polyA RNA, facilitating efficient mRNA deadenylation by the intact Pan2-Pan3 complex.
PubMed: 24872509
DOI: 10.15252/EMBJ.201488373
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 4cyk
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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