3C66

Yeast poly(A) polymerase in complex with Fip1 residues 80-105

3C66 の概要

• エントリーDOI: 10.2210/pdb3c66/pdb
• 関連するPDBエントリー: 1FA0 2HHP 2O1P 2Q66
• 分子名称: Poly(A) polymerase, Pre-mRNA polyadenylation factor FIP1, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: peptide-protein complex, mrna processing, nucleus, rna-binding, transferase, phosphoprotein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Nucleus : P29468 P45976
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 130088.04

構造登録者

Bohm, A.,Meinke, G. (登録日: 2008-02-02, 公開日: 2008-05-20, 最終更新日: 2024-02-21)

主引用文献

Meinke, G.,Ezeokonkwo, C.,Balbo, P.,Stafford, W.,Moore, C.,Bohm, A.
Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein.
Biochemistry, 47:6859-6869, 2008

PubMed Abstract: In yeast, the mRNA processing enzyme poly(A) polymerase is tethered to the much larger 3'-end processing complex via Fip1, a 36 kDa protein of unknown structure. We report the 2.6 A crystal structure of yeast poly(A) polymerase in complex with a peptide containing residues 80-105 of Fip1. The Fip1 peptide binds to the outside surface of the C-terminal domain of the polymerase. On the basis of this structure, we designed a mutant of the polymerase (V498Y, C485R) that is lethal to yeast. The mutant is unable to bind Fip1 but retains full polymerase activity. Fip1 is found in all eukaryotes and serves to connect poly(A) polymerase to pre-mRNA processing complexes in yeast, plants, and mammals. However, the Fip1 sequence is highly divergent, and residues on both Pap1 and Fip1 at the observed interaction surface are poorly conserved. Herein we demonstrate using analytical ultracentrifugation, circular dichroism, proteolytic studies, and other techniques that, in the absence of Pap1, Fip1 is largely, if not completely, unfolded. We speculate that flexibility may be important for Fip1's function as a molecular scaffold.

PubMed: 18537269
DOI: 10.1021/bi800204k

実験手法

X-RAY DIFFRACTION (2.6 Å)