4C0B

Structure of wild-type Clp1p-Pcf11p (454 -563) complex

4C0B の概要

• エントリーDOI: 10.2210/pdb4c0b/pdb
• 関連するPDBエントリー: 4C0H
• 分子名称: MRNA CLEAVAGE AND POLYADENYLATION FACTOR CLP1, PCF11P, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: transcription, 3'-end mrna processing
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Nucleus : Q08685
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 126492.51

構造登録者

Fribourg, S.,Dupin, A.F. (登録日: 2013-08-01, 公開日: 2014-02-19, 最終更新日: 2023-12-20)

主引用文献

Dupin, A.F.,Fribourg, S.
Structural basis for ATP loss by Clp1p in a G135R mutant protein.
Biochimie, 101:203-207, 2014

PubMed Abstract: Pcf11p and Clp1p form a heterodimer and are subunits of the Cleavage Factor IA (CF IA), a complex that is involved in the maturation of the 3'-end of mRNAs in Saccharomyces cerevisiae. The role of Clp1p protein in polyadenylation remains elusive, as does the need for ATP binding by Clp1p. In order to obtain structural details at atomic resolution of point mutants of Clp1p, we solved the crystal structure of Clp1-1p (G135R) point mutant complexed with Pcf11p (454-563) domain. The Clp1-1p-Pcf11p structure provides the atomic details for ATP loss while the point mutation preserves intact the Pcf11p interaction surface of Clp1p. This provides a rationale for the absence of phenotype in the yeast clp1-1 strain. Additionally, the structure allows for the description of an extended binding interface of Pcf11p with Clp1p which is likely to be S. cerevisiae specific.

PubMed: 24508575
DOI: 10.1016/j.biochi.2014.01.017

実験手法

X-RAY DIFFRACTION (2.77 Å)